---
_id: '14795'
abstract:
- lang: eng
  text: Metazoan development relies on the formation and remodeling of cell-cell contacts.
    Dynamic reorganization of adhesion receptors and the actomyosin cell cortex in
    space and time plays a central role in cell-cell contact formation and maturation.
    Nevertheless, how this process is mechanistically achieved when new contacts are
    formed remains unclear. Here, by building a biomimetic assay composed of progenitor
    cells adhering to supported lipid bilayers functionalized with E-cadherin ectodomains,
    we show that cortical F-actin flows, driven by the depletion of myosin-2 at the
    cell contact center, mediate the dynamic reorganization of adhesion receptors
    and cell cortex at the contact. E-cadherin-dependent downregulation of the small
    GTPase RhoA at the forming contact leads to both a depletion of myosin-2 and a
    decrease of F-actin at the contact center. At the contact rim, in contrast, myosin-2
    becomes enriched by the retraction of bleb-like protrusions, resulting in a cortical
    tension gradient from the contact rim to its center. This tension gradient, in
    turn, triggers centrifugal F-actin flows, leading to further accumulation of F-actin
    at the contact rim and the progressive redistribution of E-cadherin from the contact
    center to the rim. Eventually, this combination of actomyosin downregulation and
    flows at the contact determines the characteristic molecular organization, with
    E-cadherin and F-actin accumulating at the contact rim, where they are needed
    to mechanically link the contractile cortices of the adhering cells.
acknowledged_ssus:
- _id: Bio
- _id: PreCl
acknowledgement: "We are grateful to Edwin Munro for their feedback and help with
  the single particle analysis. We thank members of the Heisenberg and Loose labs
  for their help and feedback on the manuscript, notably Xin Tong for making the PCS2-mCherry-AHPH
  plasmid. Finally, we thank the Aquatics and Imaging & Optics facilities of ISTA
  for their continuous support, especially Yann Cesbron for assistance with the laser
  cutter. This work was supported by an ERC\r\nAdvanced Grant (MECSPEC) to C.-P.H."
article_processing_charge: Yes (via OA deal)
article_type: original
arxiv: 1
author:
- first_name: Feyza N
  full_name: Arslan, Feyza N
  id: 49DA7910-F248-11E8-B48F-1D18A9856A87
  last_name: Arslan
  orcid: 0000-0001-5809-9566
- first_name: Edouard B
  full_name: Hannezo, Edouard B
  id: 3A9DB764-F248-11E8-B48F-1D18A9856A87
  last_name: Hannezo
  orcid: 0000-0001-6005-1561
- first_name: Jack
  full_name: Merrin, Jack
  id: 4515C308-F248-11E8-B48F-1D18A9856A87
  last_name: Merrin
  orcid: 0000-0001-5145-4609
- first_name: Martin
  full_name: Loose, Martin
  id: 462D4284-F248-11E8-B48F-1D18A9856A87
  last_name: Loose
  orcid: 0000-0001-7309-9724
- first_name: Carl-Philipp J
  full_name: Heisenberg, Carl-Philipp J
  id: 39427864-F248-11E8-B48F-1D18A9856A87
  last_name: Heisenberg
  orcid: 0000-0002-0912-4566
citation:
  ama: Arslan FN, Hannezo EB, Merrin J, Loose M, Heisenberg C-PJ. Adhesion-induced
    cortical flows pattern E-cadherin-mediated cell contacts. <i>Current Biology</i>.
    2024;34(1):171-182.e8. doi:<a href="https://doi.org/10.1016/j.cub.2023.11.067">10.1016/j.cub.2023.11.067</a>
  apa: Arslan, F. N., Hannezo, E. B., Merrin, J., Loose, M., &#38; Heisenberg, C.-P.
    J. (2024). Adhesion-induced cortical flows pattern E-cadherin-mediated cell contacts.
    <i>Current Biology</i>. Elsevier. <a href="https://doi.org/10.1016/j.cub.2023.11.067">https://doi.org/10.1016/j.cub.2023.11.067</a>
  chicago: Arslan, Feyza N, Edouard B Hannezo, Jack Merrin, Martin Loose, and Carl-Philipp
    J Heisenberg. “Adhesion-Induced Cortical Flows Pattern E-Cadherin-Mediated Cell
    Contacts.” <i>Current Biology</i>. Elsevier, 2024. <a href="https://doi.org/10.1016/j.cub.2023.11.067">https://doi.org/10.1016/j.cub.2023.11.067</a>.
  ieee: F. N. Arslan, E. B. Hannezo, J. Merrin, M. Loose, and C.-P. J. Heisenberg,
    “Adhesion-induced cortical flows pattern E-cadherin-mediated cell contacts,” <i>Current
    Biology</i>, vol. 34, no. 1. Elsevier, p. 171–182.e8, 2024.
  ista: Arslan FN, Hannezo EB, Merrin J, Loose M, Heisenberg C-PJ. 2024. Adhesion-induced
    cortical flows pattern E-cadherin-mediated cell contacts. Current Biology. 34(1),
    171–182.e8.
  mla: Arslan, Feyza N., et al. “Adhesion-Induced Cortical Flows Pattern E-Cadherin-Mediated
    Cell Contacts.” <i>Current Biology</i>, vol. 34, no. 1, Elsevier, 2024, p. 171–182.e8,
    doi:<a href="https://doi.org/10.1016/j.cub.2023.11.067">10.1016/j.cub.2023.11.067</a>.
  short: F.N. Arslan, E.B. Hannezo, J. Merrin, M. Loose, C.-P.J. Heisenberg, Current
    Biology 34 (2024) 171–182.e8.
corr_author: '1'
date_created: 2024-01-14T23:00:56Z
date_published: 2024-01-08T00:00:00Z
date_updated: 2025-07-22T14:58:27Z
day: '08'
ddc:
- '570'
department:
- _id: CaHe
- _id: EdHa
- _id: MaLo
- _id: NanoFab
doi: 10.1016/j.cub.2023.11.067
ec_funded: 1
external_id:
  arxiv:
  - '2410.03589'
file:
- access_level: open_access
  checksum: 51220b76d72a614208f84bdbfbaf9b72
  content_type: application/pdf
  creator: dernst
  date_created: 2024-01-16T10:53:31Z
  date_updated: 2024-01-16T10:53:31Z
  file_id: '14813'
  file_name: 2024_CurrentBiology_Arslan.pdf
  file_size: 5183861
  relation: main_file
  success: 1
file_date_updated: 2024-01-16T10:53:31Z
has_accepted_license: '1'
intvolume: '        34'
issue: '1'
language:
- iso: eng
month: '01'
oa: 1
oa_version: Published Version
page: 171-182.e8
project:
- _id: 260F1432-B435-11E9-9278-68D0E5697425
  call_identifier: H2020
  grant_number: '742573'
  name: Interaction and feedback between cell mechanics and fate specification in
    vertebrate gastrulation
publication: Current Biology
publication_identifier:
  eissn:
  - 1879-0445
  issn:
  - 0960-9822
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Adhesion-induced cortical flows pattern E-cadherin-mediated cell contacts
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 34
year: '2024'
...
---
_id: '14479'
abstract:
- lang: eng
  text: 'In animals, parasitic infections impose significant fitness costs.1,2,3,4,5,6
    Infected animals can alter their feeding behavior to resist infection,7,8,9,10,11,12
    but parasites can manipulate animal foraging behavior to their own benefits.13,14,15,16
    How nutrition influences host-parasite interactions is not well understood, as
    studies have mainly focused on the host and less on the parasite.9,12,17,18,19,20,21,22,23
    We used the nutritional geometry framework24 to investigate the role of amino
    acids (AA) and carbohydrates (C) in a host-parasite system: the Argentine ant,
    Linepithema humile, and the entomopathogenic fungus, Metarhizium brunneum. First,
    using 18 diets varying in AA:C composition, we established that the fungus performed
    best on the high-amino-acid diet 1:4. Second, we found that the fungus reached
    this optimal diet when given various diet pairings, revealing its ability to cope
    with nutritional challenges. Third, we showed that the optimal fungal diet reduced
    the lifespan of healthy ants when compared with a high-carbohydrate diet but had
    no effect on infected ants. Fourth, we revealed that infected ant colonies, given
    a choice between the optimal fungal diet and a high-carbohydrate diet, chose the
    optimal fungal diet, whereas healthy colonies avoided it. Lastly, by disentangling
    fungal infection from host immune response, we demonstrated that infected ants
    foraged on the optimal fungal diet in response to immune activation and not as
    a result of parasite manipulation. Therefore, we revealed that infected ant colonies
    chose a diet that is costly for survival in the long term but beneficial in the
    short term—a form of collective self-medication.'
acknowledgement: We are sincerely grateful to the referees for their valuable comments
  and suggestions, which helped us to improve the paper. We are thankful to Jorgen
  Eilenberg and Nicolai V. Meyling for the fungal strain, to Simon Tragust, Abel Bernadou,
  and Brian Lazarro for insightful discussions, to Iago Sanmartín-Villar, Léa Briard,
  Céline Maitrel, and Nolwenn Rissen for their help with the experiments. Furthermore,
  we thank Anna V. Grasse for help with the immune gene expression analyses. We thank
  Sergio Ibarra for creating the graphical abstract. E.C. was supported by a Fyssen
  Foundation grant and the Alexander von Humboldt Foundation. A.D. was supported by
  the CNRS.
article_processing_charge: No
article_type: original
author:
- first_name: Eniko
  full_name: Csata, Eniko
  last_name: Csata
- first_name: Alfonso
  full_name: Perez-Escudero, Alfonso
  last_name: Perez-Escudero
- first_name: Emmanuel
  full_name: Laury, Emmanuel
  last_name: Laury
- first_name: Hanna
  full_name: Leitner, Hanna
  id: 8fc5c6f6-5903-11ec-abad-c83f046253e7
  last_name: Leitner
- first_name: Gerard
  full_name: Latil, Gerard
  last_name: Latil
- first_name: Juerge
  full_name: Heinze, Juerge
  last_name: Heinze
- first_name: Stephen
  full_name: Simpson, Stephen
  last_name: Simpson
- first_name: Sylvia
  full_name: Cremer, Sylvia
  id: 2F64EC8C-F248-11E8-B48F-1D18A9856A87
  last_name: Cremer
  orcid: 0000-0002-2193-3868
- first_name: Audrey
  full_name: Dussutour, Audrey
  last_name: Dussutour
citation:
  ama: Csata E, Perez-Escudero A, Laury E, et al. Fungal infection alters collective
    nutritional intake of ant colonies. <i>Current Biology</i>. 2024;34(4):902-909.e6.
    doi:<a href="https://doi.org/10.1016/j.cub.2024.01.017">10.1016/j.cub.2024.01.017</a>
  apa: Csata, E., Perez-Escudero, A., Laury, E., Leitner, H., Latil, G., Heinze, J.,
    … Dussutour, A. (2024). Fungal infection alters collective nutritional intake
    of ant colonies. <i>Current Biology</i>. Elsevier. <a href="https://doi.org/10.1016/j.cub.2024.01.017">https://doi.org/10.1016/j.cub.2024.01.017</a>
  chicago: Csata, Eniko, Alfonso Perez-Escudero, Emmanuel Laury, Hanna Leitner, Gerard
    Latil, Juerge Heinze, Stephen Simpson, Sylvia Cremer, and Audrey Dussutour. “Fungal
    Infection Alters Collective Nutritional Intake of Ant Colonies.” <i>Current Biology</i>.
    Elsevier, 2024. <a href="https://doi.org/10.1016/j.cub.2024.01.017">https://doi.org/10.1016/j.cub.2024.01.017</a>.
  ieee: E. Csata <i>et al.</i>, “Fungal infection alters collective nutritional intake
    of ant colonies,” <i>Current Biology</i>, vol. 34, no. 4. Elsevier, p. 902–909.e6,
    2024.
  ista: Csata E, Perez-Escudero A, Laury E, Leitner H, Latil G, Heinze J, Simpson
    S, Cremer S, Dussutour A. 2024. Fungal infection alters collective nutritional
    intake of ant colonies. Current Biology. 34(4), 902–909.e6.
  mla: Csata, Eniko, et al. “Fungal Infection Alters Collective Nutritional Intake
    of Ant Colonies.” <i>Current Biology</i>, vol. 34, no. 4, Elsevier, 2024, p. 902–909.e6,
    doi:<a href="https://doi.org/10.1016/j.cub.2024.01.017">10.1016/j.cub.2024.01.017</a>.
  short: E. Csata, A. Perez-Escudero, E. Laury, H. Leitner, G. Latil, J. Heinze, S.
    Simpson, S. Cremer, A. Dussutour, Current Biology 34 (2024) 902–909.e6.
dataavailabilitystatement: no DAS
date_created: 2023-10-31T13:30:20Z
date_published: 2024-02-26T00:00:00Z
date_updated: 2026-03-18T11:15:21Z
day: '26'
department:
- _id: SyCr
doi: 10.1016/j.cub.2024.01.017
external_id:
  pmid:
  - '38307022'
intvolume: '        34'
issue: '4'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1101/2023.10.26.564092
month: '02'
oa: 1
oa_version: Preprint
page: 902-909.e6
pmid: 1
publication: Current Biology
publication_identifier:
  eissn:
  - 1879-0445
  issn:
  - 0960-9822
  issnl:
  - 1234-5678
publication_status: published
publisher: Elsevier
quality_controlled: '1'
researchdata_availability: unclear
scopus_import: '1'
status: public
supplementarymaterial: yes
title: Fungal infection alters collective nutritional intake of ant colonies
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 34
year: '2024'
...
---
_id: '8824'
abstract:
- lang: eng
  text: Plants are able to orient their growth according to gravity, which ultimately
    controls both shoot and root architecture.1 Gravitropism is a dynamic process
    whereby gravistimulation induces the asymmetric distribution of the plant hormone
    auxin, leading to asymmetric growth, organ bending, and subsequent reset of auxin
    distribution back to the original pre-gravistimulation situation.1,  2,  3 Differential
    auxin accumulation during the gravitropic response depends on the activity of
    polarly localized PIN-FORMED (PIN) auxin-efflux carriers.1,  2,  3,  4 In particular,
    the timing of this dynamic response is regulated by PIN2,5,6 but the underlying
    molecular mechanisms are poorly understood. Here, we show that MEMBRANE ASSOCIATED
    KINASE REGULATOR2 (MAKR2) controls the pace of the root gravitropic response.
    We found that MAKR2 is required for the PIN2 asymmetry during gravitropism by
    acting as a negative regulator of the cell-surface signaling mediated by the receptor-like
    kinase TRANSMEMBRANE KINASE1 (TMK1).2,7,  8,  9,  10 Furthermore, we show that
    the MAKR2 inhibitory effect on TMK1 signaling is antagonized by auxin itself,
    which triggers rapid MAKR2 membrane dissociation in a TMK1-dependent manner. Our
    findings suggest that the timing of the root gravitropic response is orchestrated
    by the reversible inhibition of the TMK1 signaling pathway at the cell surface.
acknowledgement: "We thank the SiCE group for discussions and comments; S. Yalovsky,
  B. Scheres, and the NASC/ABRC collection for providing transgenic Arabidopsis lines
  and plasmids; L. Kalmbach and M. Barberon for the gift of pLOK180_pFR7m34GW; A.
  Lacroix, J. Berger, and P. Bolland for plant care; and M. Fendrych for help with
  microfluidics in the J.F. lab. We acknowledge\r\nthe contribution of the SFR Biosciences
  (UMS3444/CNRS, US8/Inser m, ENS de Lyon, UCBL) facilities: C. Lionet, E. Chatre,
  and J. Brocard at LBIPLATIM-MICROSCOPY for assistance with imaging, and V. GuegenChaignon
  and A. Page at the Protein Science Facility (PSF) for assistance with protein purification
  and mass spectrometry. Y.J. was funded by ERC\r\ngrant 3363360-APPL under FP/2007–2013.
  Y.J. and Z.L.N. were funded by an ANR- and NSF-supported ERA-CAPS project (SICOPID:
  ANR-17-CAPS0003-01/NSF PGRP IOS-1841917). A.I.C.-D. is funded by an ERC consolidator
  grant (ERC-2015-CoG–683163) and BIO2016-78955 grant from the Spanish Ministry of
  Economy and Competitiveness. Exchanges between the Y.J. and T.B. laboratories were
  funded by Tournesol grant 35656NB. B.K.M. was\r\nfunded by the Omics@vib Marie Curie
  COFUND and Research Foundation Flanders for a postdoctoral fellowship."
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: MM
  full_name: Marquès-Bueno, MM
  last_name: Marquès-Bueno
- first_name: L
  full_name: Armengot, L
  last_name: Armengot
- first_name: LC
  full_name: Noack, LC
  last_name: Noack
- first_name: J
  full_name: Bareille, J
  last_name: Bareille
- first_name: Lesia
  full_name: Rodriguez Solovey, Lesia
  id: 3922B506-F248-11E8-B48F-1D18A9856A87
  last_name: Rodriguez Solovey
  orcid: 0000-0002-7244-7237
- first_name: MP
  full_name: Platre, MP
  last_name: Platre
- first_name: V
  full_name: Bayle, V
  last_name: Bayle
- first_name: M
  full_name: Liu, M
  last_name: Liu
- first_name: D
  full_name: Opdenacker, D
  last_name: Opdenacker
- first_name: S
  full_name: Vanneste, S
  last_name: Vanneste
- first_name: BK
  full_name: Möller, BK
  last_name: Möller
- first_name: ZL
  full_name: Nimchuk, ZL
  last_name: Nimchuk
- first_name: T
  full_name: Beeckman, T
  last_name: Beeckman
- first_name: AI
  full_name: Caño-Delgado, AI
  last_name: Caño-Delgado
- first_name: Jiří
  full_name: Friml, Jiří
  id: 4159519E-F248-11E8-B48F-1D18A9856A87
  last_name: Friml
  orcid: 0000-0002-8302-7596
- first_name: Y
  full_name: Jaillais, Y
  last_name: Jaillais
citation:
  ama: Marquès-Bueno M, Armengot L, Noack L, et al. Auxin-regulated reversible inhibition
    of TMK1 signaling by MAKR2 modulates the dynamics of root gravitropism. <i>Current
    Biology</i>. 2021;31(1). doi:<a href="https://doi.org/10.1016/j.cub.2020.10.011">10.1016/j.cub.2020.10.011</a>
  apa: Marquès-Bueno, M., Armengot, L., Noack, L., Bareille, J., Rodriguez Solovey,
    L., Platre, M., … Jaillais, Y. (2021). Auxin-regulated reversible inhibition of
    TMK1 signaling by MAKR2 modulates the dynamics of root gravitropism. <i>Current
    Biology</i>. Elsevier. <a href="https://doi.org/10.1016/j.cub.2020.10.011">https://doi.org/10.1016/j.cub.2020.10.011</a>
  chicago: Marquès-Bueno, MM, L Armengot, LC Noack, J Bareille, Lesia Rodriguez Solovey,
    MP Platre, V Bayle, et al. “Auxin-Regulated Reversible Inhibition of TMK1 Signaling
    by MAKR2 Modulates the Dynamics of Root Gravitropism.” <i>Current Biology</i>.
    Elsevier, 2021. <a href="https://doi.org/10.1016/j.cub.2020.10.011">https://doi.org/10.1016/j.cub.2020.10.011</a>.
  ieee: M. Marquès-Bueno <i>et al.</i>, “Auxin-regulated reversible inhibition of
    TMK1 signaling by MAKR2 modulates the dynamics of root gravitropism,” <i>Current
    Biology</i>, vol. 31, no. 1. Elsevier, 2021.
  ista: Marquès-Bueno M, Armengot L, Noack L, Bareille J, Rodriguez Solovey L, Platre
    M, Bayle V, Liu M, Opdenacker D, Vanneste S, Möller B, Nimchuk Z, Beeckman T,
    Caño-Delgado A, Friml J, Jaillais Y. 2021. Auxin-regulated reversible inhibition
    of TMK1 signaling by MAKR2 modulates the dynamics of root gravitropism. Current
    Biology. 31(1).
  mla: Marquès-Bueno, MM, et al. “Auxin-Regulated Reversible Inhibition of TMK1 Signaling
    by MAKR2 Modulates the Dynamics of Root Gravitropism.” <i>Current Biology</i>,
    vol. 31, no. 1, Elsevier, 2021, doi:<a href="https://doi.org/10.1016/j.cub.2020.10.011">10.1016/j.cub.2020.10.011</a>.
  short: M. Marquès-Bueno, L. Armengot, L. Noack, J. Bareille, L. Rodriguez Solovey,
    M. Platre, V. Bayle, M. Liu, D. Opdenacker, S. Vanneste, B. Möller, Z. Nimchuk,
    T. Beeckman, A. Caño-Delgado, J. Friml, Y. Jaillais, Current Biology 31 (2021).
date_created: 2020-12-01T13:39:46Z
date_published: 2021-01-11T00:00:00Z
date_updated: 2023-09-05T13:03:15Z
day: '11'
ddc:
- '570'
department:
- _id: JiFr
doi: 10.1016/j.cub.2020.10.011
external_id:
  isi:
  - '000614361000039'
  pmid:
  - '33157019'
file:
- access_level: open_access
  checksum: 30b3393d841fb2b1e2b22fb42b5c8fff
  content_type: application/pdf
  creator: dernst
  date_created: 2021-02-04T11:37:50Z
  date_updated: 2021-02-04T11:37:50Z
  file_id: '9090'
  file_name: 2021_CurrentBiology_MarquesBueno.pdf
  file_size: 3458646
  relation: main_file
  success: 1
file_date_updated: 2021-02-04T11:37:50Z
has_accepted_license: '1'
intvolume: '        31'
isi: 1
issue: '1'
language:
- iso: eng
month: '01'
oa: 1
oa_version: Published Version
pmid: 1
publication: Current Biology
publication_identifier:
  eissn:
  - 1879-0445
  issn:
  - 0960-9822
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Auxin-regulated reversible inhibition of TMK1 signaling by MAKR2 modulates
  the dynamics of root gravitropism
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 31
year: '2021'
...
---
_id: '9290'
abstract:
- lang: eng
  text: Polar subcellular localization of the PIN exporters of the phytohormone auxin
    is a key determinant of directional, intercellular auxin transport and thus a
    central topic of both plant cell and developmental biology. Arabidopsis mutants
    lacking PID, a kinase that phosphorylates PINs, or the MAB4/MEL proteins of unknown
    molecular function display PIN polarity defects and phenocopy pin mutants, but
    mechanistic insights into how these factors convey PIN polarity are missing. Here,
    by combining protein biochemistry with quantitative live-cell imaging, we demonstrate
    that PINs, MAB4/MELs, and AGC kinases interact in the same complex at the plasma
    membrane. MAB4/MELs are recruited to the plasma membrane by the PINs and in concert
    with the AGC kinases maintain PIN polarity through limiting lateral diffusion-based
    escape of PINs from the polar domain. The PIN-MAB4/MEL-PID protein complex has
    self-reinforcing properties thanks to positive feedback between AGC kinase-mediated
    PIN phosphorylation and MAB4/MEL recruitment. We thus uncover the molecular mechanism
    by which AGC kinases and MAB4/MEL proteins regulate PIN localization and plant
    development.
acknowledged_ssus:
- _id: Bio
acknowledgement: We acknowledge Ben Scheres, Christian Luschnig, and Claus Schwechheimer
  for sharing published material. We thank Monika Hrtyan and Dorota Jaworska at IST
  Austria and Gerda Lamers and Ward de Winter at IBL Netherlands for technical assistance;
  Corinna Hartinger, Jakub Hajný, Lesia Rodriguez, Mingyue Li, and Lindy Abas for
  experimental support; and the Bioimaging Facility at IST Austria and the Bioimaging
  Core at VIB for imaging support. We are grateful to Christian Luschnig, Lindy Abas,
  and Roman Pleskot for valuable discussions. We also acknowledge the EMBO for supporting
  M.G. with a long-term fellowship ( ALTF 1005-2019 ) during the finalization and
  revision of this manuscript in the laboratory of B.D.R., and we thank R. Pierik
  for allowing K.V.G. to work on this manuscript during a postdoc in his laboratory
  at Utrecht University. This work was supported by grants from the European Research
  Council under the European Union’s Seventh Framework Programme (ERC grant agreements
  742985 to J.F., 714055 to B.D.R., and 803048 to M.F.), the Austrian Science Fund
  (FWF; I 3630-B25 to J.F.), Chemical Sciences (partly) financed by the Dutch Research
  Council (NWO-CW TOP 700.58.301 to R.O.), the Dutch Research Council (NWO-VICI 865.17.002
  to R. Pierik), Grants-in-Aid from the Ministry of Education, Culture, Sports, Science
  and Technology, Japan (KAKENHI grant 17K17595 to S.N.), the Ministry of Education,
  Youth and Sports of the Czech Republic (MŠMT project NPUI-LO1417 ), and a China
  Scholarship Council (to X.W.).
article_processing_charge: No
article_type: original
author:
- first_name: Matous
  full_name: Glanc, Matous
  id: 1AE1EA24-02D0-11E9-9BAA-DAF4881429F2
  last_name: Glanc
  orcid: 0000-0003-0619-7783
- first_name: K
  full_name: Van Gelderen, K
  last_name: Van Gelderen
- first_name: Lukas
  full_name: Hörmayer, Lukas
  id: 2EEE7A2A-F248-11E8-B48F-1D18A9856A87
  last_name: Hörmayer
  orcid: 0000-0001-8295-2926
- first_name: Shutang
  full_name: Tan, Shutang
  id: 2DE75584-F248-11E8-B48F-1D18A9856A87
  last_name: Tan
  orcid: 0000-0002-0471-8285
- first_name: S
  full_name: Naramoto, S
  last_name: Naramoto
- first_name: Xixi
  full_name: Zhang, Xixi
  id: 61A66458-47E9-11EA-85BA-8AEAAF14E49A
  last_name: Zhang
  orcid: 0000-0001-7048-4627
- first_name: David
  full_name: Domjan, David
  id: C684CD7A-257E-11EA-9B6F-D8588B4F947F
  last_name: Domjan
  orcid: 0000-0003-2267-106X
- first_name: L
  full_name: Vcelarova, L
  last_name: Vcelarova
- first_name: Robert
  full_name: Hauschild, Robert
  id: 4E01D6B4-F248-11E8-B48F-1D18A9856A87
  last_name: Hauschild
  orcid: 0000-0001-9843-3522
- first_name: Alexander J
  full_name: Johnson, Alexander J
  id: 46A62C3A-F248-11E8-B48F-1D18A9856A87
  last_name: Johnson
  orcid: 0000-0002-2739-8843
- first_name: E
  full_name: de Koning, E
  last_name: de Koning
- first_name: M
  full_name: van Dop, M
  last_name: van Dop
- first_name: E
  full_name: Rademacher, E
  last_name: Rademacher
- first_name: S
  full_name: Janson, S
  last_name: Janson
- first_name: X
  full_name: Wei, X
  last_name: Wei
- first_name: Gergely
  full_name: Molnar, Gergely
  id: 34F1AF46-F248-11E8-B48F-1D18A9856A87
  last_name: Molnar
- first_name: Matyas
  full_name: Fendrych, Matyas
  id: 43905548-F248-11E8-B48F-1D18A9856A87
  last_name: Fendrych
  orcid: 0000-0002-9767-8699
- first_name: B
  full_name: De Rybel, B
  last_name: De Rybel
- first_name: R
  full_name: Offringa, R
  last_name: Offringa
- first_name: Jiří
  full_name: Friml, Jiří
  id: 4159519E-F248-11E8-B48F-1D18A9856A87
  last_name: Friml
  orcid: 0000-0002-8302-7596
citation:
  ama: Glanc M, Van Gelderen K, Hörmayer L, et al. AGC kinases and MAB4/MEL proteins
    maintain PIN polarity by limiting lateral diffusion in plant cells. <i>Current
    Biology</i>. 2021;31(9):1918-1930. doi:<a href="https://doi.org/10.1016/j.cub.2021.02.028">10.1016/j.cub.2021.02.028</a>
  apa: Glanc, M., Van Gelderen, K., Hörmayer, L., Tan, S., Naramoto, S., Zhang, X.,
    … Friml, J. (2021). AGC kinases and MAB4/MEL proteins maintain PIN polarity by
    limiting lateral diffusion in plant cells. <i>Current Biology</i>. Elsevier. <a
    href="https://doi.org/10.1016/j.cub.2021.02.028">https://doi.org/10.1016/j.cub.2021.02.028</a>
  chicago: Glanc, Matous, K Van Gelderen, Lukas Hörmayer, Shutang Tan, S Naramoto,
    Xixi Zhang, David Domjan, et al. “AGC Kinases and MAB4/MEL Proteins Maintain PIN
    Polarity by Limiting Lateral Diffusion in Plant Cells.” <i>Current Biology</i>.
    Elsevier, 2021. <a href="https://doi.org/10.1016/j.cub.2021.02.028">https://doi.org/10.1016/j.cub.2021.02.028</a>.
  ieee: M. Glanc <i>et al.</i>, “AGC kinases and MAB4/MEL proteins maintain PIN polarity
    by limiting lateral diffusion in plant cells,” <i>Current Biology</i>, vol. 31,
    no. 9. Elsevier, pp. 1918–1930, 2021.
  ista: Glanc M, Van Gelderen K, Hörmayer L, Tan S, Naramoto S, Zhang X, Domjan D,
    Vcelarova L, Hauschild R, Johnson AJ, de Koning E, van Dop M, Rademacher E, Janson
    S, Wei X, Molnar G, Fendrych M, De Rybel B, Offringa R, Friml J. 2021. AGC kinases
    and MAB4/MEL proteins maintain PIN polarity by limiting lateral diffusion in plant
    cells. Current Biology. 31(9), 1918–1930.
  mla: Glanc, Matous, et al. “AGC Kinases and MAB4/MEL Proteins Maintain PIN Polarity
    by Limiting Lateral Diffusion in Plant Cells.” <i>Current Biology</i>, vol. 31,
    no. 9, Elsevier, 2021, pp. 1918–30, doi:<a href="https://doi.org/10.1016/j.cub.2021.02.028">10.1016/j.cub.2021.02.028</a>.
  short: M. Glanc, K. Van Gelderen, L. Hörmayer, S. Tan, S. Naramoto, X. Zhang, D.
    Domjan, L. Vcelarova, R. Hauschild, A.J. Johnson, E. de Koning, M. van Dop, E.
    Rademacher, S. Janson, X. Wei, G. Molnar, M. Fendrych, B. De Rybel, R. Offringa,
    J. Friml, Current Biology 31 (2021) 1918–1930.
date_created: 2021-03-26T12:09:33Z
date_published: 2021-03-10T00:00:00Z
date_updated: 2023-09-05T13:03:34Z
day: '10'
ddc:
- '580'
department:
- _id: JiFr
doi: 10.1016/j.cub.2021.02.028
ec_funded: 1
external_id:
  isi:
  - '000653077800004'
  pmid:
  - '33705718'
file:
- access_level: open_access
  checksum: b1723040ecfd8c81194185472eb62546
  content_type: application/pdf
  creator: dernst
  date_created: 2021-04-01T10:53:42Z
  date_updated: 2021-04-01T10:53:42Z
  file_id: '9303'
  file_name: 2021_CurrentBiology_Glanc.pdf
  file_size: 4324371
  relation: main_file
  success: 1
file_date_updated: 2021-04-01T10:53:42Z
has_accepted_license: '1'
intvolume: '        31'
isi: 1
issue: '9'
language:
- iso: eng
month: '03'
oa: 1
oa_version: Published Version
page: 1918-1930
pmid: 1
project:
- _id: 261099A6-B435-11E9-9278-68D0E5697425
  call_identifier: H2020
  grant_number: '742985'
  name: Tracing Evolution of Auxin Transport and Polarity in Plants
- _id: 26538374-B435-11E9-9278-68D0E5697425
  call_identifier: FWF
  grant_number: I03630
  name: Molecular mechanisms of endocytic cargo recognition in plants
publication: Current Biology
publication_identifier:
  eissn:
  - 1879-0445
  issn:
  - 0960-9822
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: AGC kinases and MAB4/MEL proteins maintain PIN polarity by limiting lateral
  diffusion in plant cells
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 31
year: '2021'
...
---
_id: '6979'
article_processing_charge: No
article_type: original
author:
- first_name: Aglaja
  full_name: Kopf, Aglaja
  id: 31DAC7B6-F248-11E8-B48F-1D18A9856A87
  last_name: Kopf
  orcid: 0000-0002-2187-6656
- first_name: Michael K
  full_name: Sixt, Michael K
  id: 41E9FBEA-F248-11E8-B48F-1D18A9856A87
  last_name: Sixt
  orcid: 0000-0002-6620-9179
citation:
  ama: 'Kopf A, Sixt MK. Gut homeostasis: Active migration of intestinal epithelial
    cells in tissue renewal. <i>Current Biology</i>. 2019;29(20):R1091-R1093. doi:<a
    href="https://doi.org/10.1016/j.cub.2019.08.068">10.1016/j.cub.2019.08.068</a>'
  apa: 'Kopf, A., &#38; Sixt, M. K. (2019). Gut homeostasis: Active migration of intestinal
    epithelial cells in tissue renewal. <i>Current Biology</i>. Cell Press. <a href="https://doi.org/10.1016/j.cub.2019.08.068">https://doi.org/10.1016/j.cub.2019.08.068</a>'
  chicago: 'Kopf, Aglaja, and Michael K Sixt. “Gut Homeostasis: Active Migration of
    Intestinal Epithelial Cells in Tissue Renewal.” <i>Current Biology</i>. Cell Press,
    2019. <a href="https://doi.org/10.1016/j.cub.2019.08.068">https://doi.org/10.1016/j.cub.2019.08.068</a>.'
  ieee: 'A. Kopf and M. K. Sixt, “Gut homeostasis: Active migration of intestinal
    epithelial cells in tissue renewal,” <i>Current Biology</i>, vol. 29, no. 20.
    Cell Press, pp. R1091–R1093, 2019.'
  ista: 'Kopf A, Sixt MK. 2019. Gut homeostasis: Active migration of intestinal epithelial
    cells in tissue renewal. Current Biology. 29(20), R1091–R1093.'
  mla: 'Kopf, Aglaja, and Michael K. Sixt. “Gut Homeostasis: Active Migration of Intestinal
    Epithelial Cells in Tissue Renewal.” <i>Current Biology</i>, vol. 29, no. 20,
    Cell Press, 2019, pp. R1091–93, doi:<a href="https://doi.org/10.1016/j.cub.2019.08.068">10.1016/j.cub.2019.08.068</a>.'
  short: A. Kopf, M.K. Sixt, Current Biology 29 (2019) R1091–R1093.
date_created: 2019-11-04T15:18:29Z
date_published: 2019-10-21T00:00:00Z
date_updated: 2023-09-05T12:43:43Z
day: '21'
department:
- _id: MiSi
doi: 10.1016/j.cub.2019.08.068
external_id:
  isi:
  - '000491286200016'
  pmid:
  - '31639357'
intvolume: '        29'
isi: 1
issue: '20'
language:
- iso: eng
month: '10'
oa_version: None
page: R1091-R1093
pmid: 1
publication: Current Biology
publication_identifier:
  eissn:
  - 1879-0445
  issn:
  - 0960-9822
publication_status: published
publisher: Cell Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Gut homeostasis: Active migration of intestinal epithelial cells in tissue
  renewal'
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 29
year: '2019'
...
---
_id: '9489'
abstract:
- lang: eng
  text: Cytosine methylation is an ancient process with conserved enzymology but diverse
    biological functions that include defense against transposable elements and regulation
    of gene expression. Here we will discuss the evolution and biological significance
    of eukaryotic DNA methylation, the likely drivers of that evolution, and major
    remaining mysteries.
article_processing_charge: No
article_type: review
author:
- first_name: Assaf
  full_name: Zemach, Assaf
  last_name: Zemach
- first_name: Daniel
  full_name: Zilberman, Daniel
  id: 6973db13-dd5f-11ea-814e-b3e5455e9ed1
  last_name: Zilberman
  orcid: 0000-0002-0123-8649
citation:
  ama: Zemach A, Zilberman D. Evolution of eukaryotic DNA methylation and the pursuit
    of safer sex. <i>Current Biology</i>. 2010;20(17):R780-R785. doi:<a href="https://doi.org/10.1016/j.cub.2010.07.007">10.1016/j.cub.2010.07.007</a>
  apa: Zemach, A., &#38; Zilberman, D. (2010). Evolution of eukaryotic DNA methylation
    and the pursuit of safer sex. <i>Current Biology</i>. Elsevier. <a href="https://doi.org/10.1016/j.cub.2010.07.007">https://doi.org/10.1016/j.cub.2010.07.007</a>
  chicago: Zemach, Assaf, and Daniel Zilberman. “Evolution of Eukaryotic DNA Methylation
    and the Pursuit of Safer Sex.” <i>Current Biology</i>. Elsevier, 2010. <a href="https://doi.org/10.1016/j.cub.2010.07.007">https://doi.org/10.1016/j.cub.2010.07.007</a>.
  ieee: A. Zemach and D. Zilberman, “Evolution of eukaryotic DNA methylation and the
    pursuit of safer sex,” <i>Current Biology</i>, vol. 20, no. 17. Elsevier, pp.
    R780–R785, 2010.
  ista: Zemach A, Zilberman D. 2010. Evolution of eukaryotic DNA methylation and the
    pursuit of safer sex. Current Biology. 20(17), R780–R785.
  mla: Zemach, Assaf, and Daniel Zilberman. “Evolution of Eukaryotic DNA Methylation
    and the Pursuit of Safer Sex.” <i>Current Biology</i>, vol. 20, no. 17, Elsevier,
    2010, pp. R780–85, doi:<a href="https://doi.org/10.1016/j.cub.2010.07.007">10.1016/j.cub.2010.07.007</a>.
  short: A. Zemach, D. Zilberman, Current Biology 20 (2010) R780–R785.
date_created: 2021-06-07T09:45:27Z
date_published: 2010-09-14T00:00:00Z
date_updated: 2021-12-14T08:52:34Z
day: '14'
department:
- _id: DaZi
doi: 10.1016/j.cub.2010.07.007
extern: '1'
external_id:
  pmid:
  - '20833323'
intvolume: '        20'
issue: '17'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1016/j.cub.2010.07.007
month: '09'
oa: 1
oa_version: Published Version
page: R780-R785
pmid: 1
publication: Current Biology
publication_identifier:
  eissn:
  - 1879-0445
  issn:
  - 0960-9822
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Evolution of eukaryotic DNA methylation and the pursuit of safer sex
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 20
year: '2010'
...
---
_id: '9491'
abstract:
- lang: eng
  text: Cytosine DNA methylation in vertebrates is widespread, but methylation in
    plants is found almost exclusively at transposable elements and repetitive DNA
    [1]. Within regions of methylation, methylcytosines are typically found in CG,
    CNG, and asymmetric contexts. CG sites are maintained by a plant homolog of mammalian
    Dnmt1 acting on hemi-methylated DNA after replication. Methylation of CNG and
    asymmetric sites appears to be maintained at each cell cycle by other mechanisms.
    We report a new type of DNA methylation in Arabidopsis, dense CG methylation clusters
    found at scattered sites throughout the genome. These clusters lack non-CG methylation
    and are preferentially found in genes, although they are relatively deficient
    toward the 5′ end. CG methylation clusters are present in lines derived from different
    accessions and in mutants that eliminate de novo methylation, indicating that
    CG methylation clusters are stably maintained at specific sites. Because 5-methylcytosine
    is mutagenic, the appearance of CG methylation clusters over evolutionary time
    predicts a genome-wide deficiency of CG dinucleotides and an excess of C(A/T)G
    trinucleotides within transcribed regions. This is exactly what we find, implying
    that CG methylation clusters have contributed profoundly to plant gene evolution.
    We suggest that CG methylation clusters silence cryptic promoters that arise sporadically
    within transcription units.
article_processing_charge: No
article_type: original
author:
- first_name: Robert K.
  full_name: Tran, Robert K.
  last_name: Tran
- first_name: Jorja G.
  full_name: Henikoff, Jorja G.
  last_name: Henikoff
- first_name: Daniel
  full_name: Zilberman, Daniel
  id: 6973db13-dd5f-11ea-814e-b3e5455e9ed1
  last_name: Zilberman
  orcid: 0000-0002-0123-8649
- first_name: Renata F.
  full_name: Ditt, Renata F.
  last_name: Ditt
- first_name: Steven E.
  full_name: Jacobsen, Steven E.
  last_name: Jacobsen
- first_name: Steven
  full_name: Henikoff, Steven
  last_name: Henikoff
citation:
  ama: Tran RK, Henikoff JG, Zilberman D, Ditt RF, Jacobsen SE, Henikoff S. DNA methylation
    profiling identifies CG methylation clusters in Arabidopsis genes. <i>Current
    Biology</i>. 2005;15(2):154-159. doi:<a href="https://doi.org/10.1016/j.cub.2005.01.008">10.1016/j.cub.2005.01.008</a>
  apa: Tran, R. K., Henikoff, J. G., Zilberman, D., Ditt, R. F., Jacobsen, S. E.,
    &#38; Henikoff, S. (2005). DNA methylation profiling identifies CG methylation
    clusters in Arabidopsis genes. <i>Current Biology</i>. Elsevier. <a href="https://doi.org/10.1016/j.cub.2005.01.008">https://doi.org/10.1016/j.cub.2005.01.008</a>
  chicago: Tran, Robert K., Jorja G. Henikoff, Daniel Zilberman, Renata F. Ditt, Steven
    E. Jacobsen, and Steven Henikoff. “DNA Methylation Profiling Identifies CG Methylation
    Clusters in Arabidopsis Genes.” <i>Current Biology</i>. Elsevier, 2005. <a href="https://doi.org/10.1016/j.cub.2005.01.008">https://doi.org/10.1016/j.cub.2005.01.008</a>.
  ieee: R. K. Tran, J. G. Henikoff, D. Zilberman, R. F. Ditt, S. E. Jacobsen, and
    S. Henikoff, “DNA methylation profiling identifies CG methylation clusters in
    Arabidopsis genes,” <i>Current Biology</i>, vol. 15, no. 2. Elsevier, pp. 154–159,
    2005.
  ista: Tran RK, Henikoff JG, Zilberman D, Ditt RF, Jacobsen SE, Henikoff S. 2005.
    DNA methylation profiling identifies CG methylation clusters in Arabidopsis genes.
    Current Biology. 15(2), 154–159.
  mla: Tran, Robert K., et al. “DNA Methylation Profiling Identifies CG Methylation
    Clusters in Arabidopsis Genes.” <i>Current Biology</i>, vol. 15, no. 2, Elsevier,
    2005, pp. 154–59, doi:<a href="https://doi.org/10.1016/j.cub.2005.01.008">10.1016/j.cub.2005.01.008</a>.
  short: R.K. Tran, J.G. Henikoff, D. Zilberman, R.F. Ditt, S.E. Jacobsen, S. Henikoff,
    Current Biology 15 (2005) 154–159.
date_created: 2021-06-07T10:24:30Z
date_published: 2005-01-26T00:00:00Z
date_updated: 2021-12-14T09:12:26Z
day: '26'
department:
- _id: DaZi
doi: 10.1016/j.cub.2005.01.008
extern: '1'
external_id:
  pmid:
  - '15668172 '
intvolume: '        15'
issue: '2'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1016/j.cub.2005.01.008
month: '01'
oa: 1
oa_version: Published Version
page: 154-159
pmid: 1
publication: Current Biology
publication_identifier:
  eissn:
  - 1879-0445
  issn:
  - 0960-9822
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: DNA methylation profiling identifies CG methylation clusters in Arabidopsis
  genes
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 15
year: '2005'
...
---
_id: '9493'
abstract:
- lang: eng
  text: In a number of organisms, transgenes containing transcribed inverted repeats
    (IRs) that produce hairpin RNA can trigger RNA-mediated silencing, which is associated
    with 21-24 nucleotide small interfering RNAs (siRNAs). In plants, IR-driven RNA
    silencing also causes extensive cytosine methylation of homologous DNA in both
    the transgene "trigger" and any other homologous DNA sequences--"targets". Endogenous
    genomic sequences, including transposable elements and repeated elements, are
    also subject to RNA-mediated silencing. The RNA silencing gene ARGONAUTE4 (AGO4)
    is required for maintenance of DNA methylation at several endogenous loci and
    for the establishment of methylation at the FWA gene. Here, we show that mutation
    of AGO4 substantially reduces the maintenance of DNA methylation triggered by
    IR transgenes, but AGO4 loss-of-function does not block the initiation of DNA
    methylation by IRs. AGO4 primarily affects non-CG methylation of the target sequences,
    while the IR trigger sequences lose methylation in all sequence contexts. Finally,
    we find that AGO4 and the DRM methyltransferase genes are required for maintenance
    of siRNAs at a subset of endogenous sequences, but AGO4 is not required for the
    accumulation of IR-induced siRNAs or a number of endogenous siRNAs, suggesting
    that AGO4 may function downstream of siRNA production.
article_processing_charge: No
article_type: original
author:
- first_name: Daniel
  full_name: Zilberman, Daniel
  id: 6973db13-dd5f-11ea-814e-b3e5455e9ed1
  last_name: Zilberman
  orcid: 0000-0002-0123-8649
- first_name: Xiaofeng
  full_name: Cao, Xiaofeng
  last_name: Cao
- first_name: Lisa K.
  full_name: Johansen, Lisa K.
  last_name: Johansen
- first_name: Zhixin
  full_name: Xie, Zhixin
  last_name: Xie
- first_name: James C.
  full_name: Carrington, James C.
  last_name: Carrington
- first_name: Steven E.
  full_name: Jacobsen, Steven E.
  last_name: Jacobsen
citation:
  ama: Zilberman D, Cao X, Johansen LK, Xie Z, Carrington JC, Jacobsen SE. Role of
    Arabidopsis ARGONAUTE4 in RNA-directed DNA methylation triggered by inverted repeats.
    <i>Current Biology</i>. 2004;14(13):1214-1220. doi:<a href="https://doi.org/10.1016/j.cub.2004.06.055">10.1016/j.cub.2004.06.055</a>
  apa: Zilberman, D., Cao, X., Johansen, L. K., Xie, Z., Carrington, J. C., &#38;
    Jacobsen, S. E. (2004). Role of Arabidopsis ARGONAUTE4 in RNA-directed DNA methylation
    triggered by inverted repeats. <i>Current Biology</i>. Elsevier. <a href="https://doi.org/10.1016/j.cub.2004.06.055">https://doi.org/10.1016/j.cub.2004.06.055</a>
  chicago: Zilberman, Daniel, Xiaofeng Cao, Lisa K. Johansen, Zhixin Xie, James C.
    Carrington, and Steven E. Jacobsen. “Role of Arabidopsis ARGONAUTE4 in RNA-Directed
    DNA Methylation Triggered by Inverted Repeats.” <i>Current Biology</i>. Elsevier,
    2004. <a href="https://doi.org/10.1016/j.cub.2004.06.055">https://doi.org/10.1016/j.cub.2004.06.055</a>.
  ieee: D. Zilberman, X. Cao, L. K. Johansen, Z. Xie, J. C. Carrington, and S. E.
    Jacobsen, “Role of Arabidopsis ARGONAUTE4 in RNA-directed DNA methylation triggered
    by inverted repeats,” <i>Current Biology</i>, vol. 14, no. 13. Elsevier, pp. 1214–1220,
    2004.
  ista: Zilberman D, Cao X, Johansen LK, Xie Z, Carrington JC, Jacobsen SE. 2004.
    Role of Arabidopsis ARGONAUTE4 in RNA-directed DNA methylation triggered by inverted
    repeats. Current Biology. 14(13), 1214–1220.
  mla: Zilberman, Daniel, et al. “Role of Arabidopsis ARGONAUTE4 in RNA-Directed DNA
    Methylation Triggered by Inverted Repeats.” <i>Current Biology</i>, vol. 14, no.
    13, Elsevier, 2004, pp. 1214–20, doi:<a href="https://doi.org/10.1016/j.cub.2004.06.055">10.1016/j.cub.2004.06.055</a>.
  short: D. Zilberman, X. Cao, L.K. Johansen, Z. Xie, J.C. Carrington, S.E. Jacobsen,
    Current Biology 14 (2004) 1214–1220.
date_created: 2021-06-07T10:33:00Z
date_published: 2004-07-13T00:00:00Z
date_updated: 2021-12-14T08:52:00Z
day: '13'
department:
- _id: DaZi
doi: 10.1016/j.cub.2004.06.055
extern: '1'
external_id:
  pmid:
  - '15242620 '
intvolume: '        14'
issue: '13'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1016/j.cub.2004.06.055
month: '07'
oa: 1
oa_version: Published Version
page: 1214-1220
pmid: 1
publication: Current Biology
publication_identifier:
  eissn:
  - 1879-0445
  issn:
  - 0960-9822
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Role of Arabidopsis ARGONAUTE4 in RNA-directed DNA methylation triggered by
  inverted repeats
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 14
year: '2004'
...
---
_id: '9495'
abstract:
- lang: eng
  text: RNA interference is a conserved process in which double-stranded RNA is processed
    into 21–25 nucleotide siRNAs that trigger posttranscriptional gene silencing.
    In addition, plants display a phenomenon termed RNA-directed DNA methylation (RdDM)
    in which DNA with sequence identity to silenced RNA is de novo methylated at its
    cytosine residues. This methylation is not only at canonical CpG sites but also
    at cytosines in CpNpG and asymmetric sequence contexts. In this report, we study
    the role of the DRM and CMT3 DNA methyltransferase genes in the initiation and
    maintenance of RdDM. Neither drm nor cmt3 mutants affected the maintenance of
    preestablished RNA-directed CpG methylation. However, drm mutants showed a nearly
    complete loss of asymmetric methylation and a partial loss of CpNpG methylation.
    The remaining asymmetric and CpNpG methylation was dependent on the activity of
    CMT3, showing that DRM and CMT3 act redundantly to maintain non-CpG methylation.
    These DNA methyltransferases appear to act downstream of siRNAs, since drm1 drm2
    cmt3 triple mutants show a lack of non-CpG methylation but elevated levels of
    siRNAs. Finally, we demonstrate that DRM activity is required for the initial
    establishment of RdDM in all sequence contexts including CpG, CpNpG, and asymmetric
    sites.
article_processing_charge: No
article_type: original
author:
- first_name: Xiaofeng
  full_name: Cao, Xiaofeng
  last_name: Cao
- first_name: Werner
  full_name: Aufsatz, Werner
  last_name: Aufsatz
- first_name: Daniel
  full_name: Zilberman, Daniel
  id: 6973db13-dd5f-11ea-814e-b3e5455e9ed1
  last_name: Zilberman
  orcid: 0000-0002-0123-8649
- first_name: M.Florian
  full_name: Mette, M.Florian
  last_name: Mette
- first_name: Michael S.
  full_name: Huang, Michael S.
  last_name: Huang
- first_name: Marjori
  full_name: Matzke, Marjori
  last_name: Matzke
- first_name: Steven E.
  full_name: Jacobsen, Steven E.
  last_name: Jacobsen
citation:
  ama: Cao X, Aufsatz W, Zilberman D, et al. Role of the DRM and CMT3 methyltransferases
    in RNA-directed DNA methylation. <i>Current Biology</i>. 2003;13(24):2212-2217.
    doi:<a href="https://doi.org/10.1016/j.cub.2003.11.052">10.1016/j.cub.2003.11.052</a>
  apa: Cao, X., Aufsatz, W., Zilberman, D., Mette, M. F., Huang, M. S., Matzke, M.,
    &#38; Jacobsen, S. E. (2003). Role of the DRM and CMT3 methyltransferases in RNA-directed
    DNA methylation. <i>Current Biology</i>. Elsevier. <a href="https://doi.org/10.1016/j.cub.2003.11.052">https://doi.org/10.1016/j.cub.2003.11.052</a>
  chicago: Cao, Xiaofeng, Werner Aufsatz, Daniel Zilberman, M.Florian Mette, Michael
    S. Huang, Marjori Matzke, and Steven E. Jacobsen. “Role of the DRM and CMT3 Methyltransferases
    in RNA-Directed DNA Methylation.” <i>Current Biology</i>. Elsevier, 2003. <a href="https://doi.org/10.1016/j.cub.2003.11.052">https://doi.org/10.1016/j.cub.2003.11.052</a>.
  ieee: X. Cao <i>et al.</i>, “Role of the DRM and CMT3 methyltransferases in RNA-directed
    DNA methylation,” <i>Current Biology</i>, vol. 13, no. 24. Elsevier, pp. 2212–2217,
    2003.
  ista: Cao X, Aufsatz W, Zilberman D, Mette MF, Huang MS, Matzke M, Jacobsen SE.
    2003. Role of the DRM and CMT3 methyltransferases in RNA-directed DNA methylation.
    Current Biology. 13(24), 2212–2217.
  mla: Cao, Xiaofeng, et al. “Role of the DRM and CMT3 Methyltransferases in RNA-Directed
    DNA Methylation.” <i>Current Biology</i>, vol. 13, no. 24, Elsevier, 2003, pp.
    2212–17, doi:<a href="https://doi.org/10.1016/j.cub.2003.11.052">10.1016/j.cub.2003.11.052</a>.
  short: X. Cao, W. Aufsatz, D. Zilberman, M.F. Mette, M.S. Huang, M. Matzke, S.E.
    Jacobsen, Current Biology 13 (2003) 2212–2217.
date_created: 2021-06-07T10:43:02Z
date_published: 2003-12-16T00:00:00Z
date_updated: 2021-12-14T08:41:38Z
day: '16'
department:
- _id: DaZi
doi: 10.1016/j.cub.2003.11.052
extern: '1'
external_id:
  pmid:
  - '14680640'
intvolume: '        13'
issue: '24'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1016/j.cub.2003.11.052
month: '12'
oa: 1
oa_version: Published Version
page: 2212-2217
pmid: 1
publication: Current Biology
publication_identifier:
  eissn:
  - 1879-0445
  issn:
  - 0960-9822
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Role of the DRM and CMT3 methyltransferases in RNA-directed DNA methylation
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 13
year: '2003'
...
---
_id: '4169'
abstract:
- lang: eng
  text: 'Background: During vertebrate gastrulation, cell polarization and migration
    are core components in the cellular rearrangements that lead to the formation
    of the three germ layers, ectoderm, mesoderm, and endoderm. Previous studies have
    implicated the Wnt/planar cell polarity (PCP) signaling pathway in controlling
    cell morphology and movement during gastrulation. However, cell polarization and
    directed cell migration are reduced but not completely abolished in the absence
    of Wnt/PCP signals; this observation indicates that other signaling pathways must
    be involved. Results: We show that Phosphoinositide 3-Kinases (PI3Ks) are required
    at the onset of zebrafish gastrulation in mesendodermal cells for process formation
    and cell polarization. Platelet Derived Growth Factor (PDGF) functions upstream
    of PI3K, while Protein Kinase B (PKB), a downstream effector of PI3K activity,
    localizes to the leading edge of migrating mesendodermal cells. In the absence
    of PI3K activity, PKB localization and cell polarization are strongly reduced
    in mesendodermal cells and are followed by slower but still highly coordinated
    and directed movements of these cells. Conclusions: We have identified a novel
    role of a signaling pathway comprised of PDGF, PI3K, and PKB in the control of
    morphogenetic cell movements during gastrulation. Furthermore, our findings provide
    insight into the relationship between cell polarization and directed cell migration
    at the onset of zebrafish gastrulation.'
acknowledgement: 'We would like to thank Jennifer Geiger, Juan Hurl& Hannu Mansu-koski,
  Florian Raible, Marino Zerial, Steve Wilson, and Kurt Anderson for critical reading
  of earlier versions of this manuscript. We thank Erez Raz, Bart Vanhaesebroeck,
  and Lukas Roth for sending us the pCS2-PH-GFP-nos, the p1IOCAAX, and the pCS2-actin-GFP
  constructs, respectively. We are grateful to Marino Zerial and his lab for encouraging
  us to start this work and providing us with the dnP13K construct and to Florian
  Ulrich and Franziska Friedrich for help with the confocal microscope and artwork,
  respectively. We thank Gunter Junghanns and Evelyn Lehmann for excellent fish care.
  C.-P.H. is supported by an Emmy-Noother-Fellowship from the Deutsche Forschungsgemeinschaft. '
article_processing_charge: No
article_type: original
author:
- first_name: Juan
  full_name: Montero, Juan
  last_name: Montero
- first_name: Beate
  full_name: Kilian, Beate
  last_name: Kilian
- first_name: Joanne
  full_name: Chan, Joanne
  last_name: Chan
- first_name: Peter
  full_name: Bayliss, Peter
  last_name: Bayliss
- first_name: Carl-Philipp J
  full_name: Heisenberg, Carl-Philipp J
  id: 39427864-F248-11E8-B48F-1D18A9856A87
  last_name: Heisenberg
  orcid: 0000-0002-0912-4566
citation:
  ama: Montero J, Kilian B, Chan J, Bayliss P, Heisenberg C-PJ. Phosphoinositide 3-kinase
    is required for process outgrowth and cell polarization of gastrulating mesendodermal
    cells. <i>Current Biology</i>. 2003;13(15):1279-1289. doi:<a href="https://doi.org/10.1016/S0960-9822(03)00505-0">10.1016/S0960-9822(03)00505-0</a>
  apa: Montero, J., Kilian, B., Chan, J., Bayliss, P., &#38; Heisenberg, C.-P. J.
    (2003). Phosphoinositide 3-kinase is required for process outgrowth and cell polarization
    of gastrulating mesendodermal cells. <i>Current Biology</i>. Cell Press. <a href="https://doi.org/10.1016/S0960-9822(03)00505-0">https://doi.org/10.1016/S0960-9822(03)00505-0</a>
  chicago: Montero, Juan, Beate Kilian, Joanne Chan, Peter Bayliss, and Carl-Philipp
    J Heisenberg. “Phosphoinositide 3-Kinase Is Required for Process Outgrowth and
    Cell Polarization of Gastrulating Mesendodermal Cells.” <i>Current Biology</i>.
    Cell Press, 2003. <a href="https://doi.org/10.1016/S0960-9822(03)00505-0">https://doi.org/10.1016/S0960-9822(03)00505-0</a>.
  ieee: J. Montero, B. Kilian, J. Chan, P. Bayliss, and C.-P. J. Heisenberg, “Phosphoinositide
    3-kinase is required for process outgrowth and cell polarization of gastrulating
    mesendodermal cells,” <i>Current Biology</i>, vol. 13, no. 15. Cell Press, pp.
    1279–1289, 2003.
  ista: Montero J, Kilian B, Chan J, Bayliss P, Heisenberg C-PJ. 2003. Phosphoinositide
    3-kinase is required for process outgrowth and cell polarization of gastrulating
    mesendodermal cells. Current Biology. 13(15), 1279–1289.
  mla: Montero, Juan, et al. “Phosphoinositide 3-Kinase Is Required for Process Outgrowth
    and Cell Polarization of Gastrulating Mesendodermal Cells.” <i>Current Biology</i>,
    vol. 13, no. 15, Cell Press, 2003, pp. 1279–89, doi:<a href="https://doi.org/10.1016/S0960-9822(03)00505-0">10.1016/S0960-9822(03)00505-0</a>.
  short: J. Montero, B. Kilian, J. Chan, P. Bayliss, C.-P.J. Heisenberg, Current Biology
    13 (2003) 1279–1289.
date_created: 2018-12-11T12:07:22Z
date_published: 2003-08-05T00:00:00Z
date_updated: 2024-02-27T10:03:37Z
day: '05'
doi: 10.1016/S0960-9822(03)00505-0
extern: '1'
external_id:
  pmid:
  - ' 12906787'
intvolume: '        13'
issue: '15'
language:
- iso: eng
month: '08'
oa_version: None
page: 1279 - 1289
pmid: 1
publication: Current Biology
publication_identifier:
  eissn:
  - 1879-0445
  issn:
  - 0960-9822
publication_status: published
publisher: Cell Press
publist_id: '1950'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Phosphoinositide 3-kinase is required for process outgrowth and cell polarization
  of gastrulating mesendodermal cells
type: journal_article
user_id: ea97e931-d5af-11eb-85d4-e6957dddbf17
volume: 13
year: '2003'
...
