---
_id: '14826'
abstract:
- lang: eng
  text: The plant-signaling molecule auxin triggers fast and slow cellular responses
    across land plants and algae. The nuclear auxin pathway mediates gene expression
    and controls growth and development in land plants, but this pathway is absent
    from algal sister groups. Several components of rapid responses have been identified
    in Arabidopsis, but it is unknown if these are part of a conserved mechanism.
    We recently identified a fast, proteome-wide phosphorylation response to auxin.
    Here, we show that this response occurs across 5 land plant and algal species
    and converges on a core group of shared targets. We found conserved rapid physiological
    responses to auxin in the same species and identified rapidly accelerated fibrosarcoma
    (RAF)-like protein kinases as central mediators of auxin-triggered phosphorylation
    across species. Genetic analysis connects this kinase to both auxin-triggered
    protein phosphorylation and rapid cellular response, thus identifying an ancient
    mechanism for fast auxin responses in the green lineage.
acknowledgement: 'We are grateful to Asuka Shitaku and Eri Koide for generating and
  sharing the Marchantia PRAF-mCitrine line and Peng-Cheng Wang for sharing the Arabidopsis
  raf mutant. We are grateful to our team members for discussions and helpful advice.
  This work was supported by funding from the Netherlands Organization for Scientific
  Research (NWO): VICI grant 865.14.001 and ENW-KLEIN OCENW.KLEIN.027 grants to D.W.;
  VENI grant VI.VENI.212.003 to A.K.; the European Research Council AdG DIRNDL (contract
  number 833867) to D.W.; CoG CATCH to J.S.; StG CELLONGATE (contract 803048) to M.F.;
  and AdG ETAP (contract 742985) to J.F.; MEXT KAKENHI grant number JP19H05675 to
  T.K.; JSPS KAKENHI grant number JP20H03275 to R.N.; Takeda Science Foundation to
  R.N.; and the Austrian Science Fund (FWF, P29988) to J.F.'
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Andre
  full_name: Kuhn, Andre
  last_name: Kuhn
- first_name: Mark
  full_name: Roosjen, Mark
  last_name: Roosjen
- first_name: Sumanth
  full_name: Mutte, Sumanth
  last_name: Mutte
- first_name: Shiv Mani
  full_name: Dubey, Shiv Mani
  last_name: Dubey
- first_name: Vanessa Polet
  full_name: Carrillo Carrasco, Vanessa Polet
  last_name: Carrillo Carrasco
- first_name: Sjef
  full_name: Boeren, Sjef
  last_name: Boeren
- first_name: Aline
  full_name: Monzer, Aline
  id: 2DB5D88C-D7B3-11E9-B8FD-7907E6697425
  last_name: Monzer
- first_name: Jasper
  full_name: Koehorst, Jasper
  last_name: Koehorst
- first_name: Takayuki
  full_name: Kohchi, Takayuki
  last_name: Kohchi
- first_name: Ryuichi
  full_name: Nishihama, Ryuichi
  last_name: Nishihama
- first_name: Matyas
  full_name: Fendrych, Matyas
  id: 43905548-F248-11E8-B48F-1D18A9856A87
  last_name: Fendrych
  orcid: 0000-0002-9767-8699
- first_name: Joris
  full_name: Sprakel, Joris
  last_name: Sprakel
- first_name: Jiří
  full_name: Friml, Jiří
  id: 4159519E-F248-11E8-B48F-1D18A9856A87
  last_name: Friml
  orcid: 0000-0002-8302-7596
- first_name: Dolf
  full_name: Weijers, Dolf
  last_name: Weijers
citation:
  ama: Kuhn A, Roosjen M, Mutte S, et al. RAF-like protein kinases mediate a deeply
    conserved, rapid auxin response. <i>Cell</i>. 2024;187(1):130-148.e17. doi:<a
    href="https://doi.org/10.1016/j.cell.2023.11.021">10.1016/j.cell.2023.11.021</a>
  apa: Kuhn, A., Roosjen, M., Mutte, S., Dubey, S. M., Carrillo Carrasco, V. P., Boeren,
    S., … Weijers, D. (2024). RAF-like protein kinases mediate a deeply conserved,
    rapid auxin response. <i>Cell</i>. Elsevier. <a href="https://doi.org/10.1016/j.cell.2023.11.021">https://doi.org/10.1016/j.cell.2023.11.021</a>
  chicago: Kuhn, Andre, Mark Roosjen, Sumanth Mutte, Shiv Mani Dubey, Vanessa Polet
    Carrillo Carrasco, Sjef Boeren, Aline Monzer, et al. “RAF-like Protein Kinases
    Mediate a Deeply Conserved, Rapid Auxin Response.” <i>Cell</i>. Elsevier, 2024.
    <a href="https://doi.org/10.1016/j.cell.2023.11.021">https://doi.org/10.1016/j.cell.2023.11.021</a>.
  ieee: A. Kuhn <i>et al.</i>, “RAF-like protein kinases mediate a deeply conserved,
    rapid auxin response,” <i>Cell</i>, vol. 187, no. 1. Elsevier, p. 130–148.e17,
    2024.
  ista: Kuhn A, Roosjen M, Mutte S, Dubey SM, Carrillo Carrasco VP, Boeren S, Monzer
    A, Koehorst J, Kohchi T, Nishihama R, Fendrych M, Sprakel J, Friml J, Weijers
    D. 2024. RAF-like protein kinases mediate a deeply conserved, rapid auxin response.
    Cell. 187(1), 130–148.e17.
  mla: Kuhn, Andre, et al. “RAF-like Protein Kinases Mediate a Deeply Conserved, Rapid
    Auxin Response.” <i>Cell</i>, vol. 187, no. 1, Elsevier, 2024, p. 130–148.e17,
    doi:<a href="https://doi.org/10.1016/j.cell.2023.11.021">10.1016/j.cell.2023.11.021</a>.
  short: A. Kuhn, M. Roosjen, S. Mutte, S.M. Dubey, V.P. Carrillo Carrasco, S. Boeren,
    A. Monzer, J. Koehorst, T. Kohchi, R. Nishihama, M. Fendrych, J. Sprakel, J. Friml,
    D. Weijers, Cell 187 (2024) 130–148.e17.
date_created: 2024-01-17T12:45:40Z
date_published: 2024-01-04T00:00:00Z
date_updated: 2024-01-22T13:43:40Z
day: '04'
ddc:
- '580'
department:
- _id: JiFr
doi: 10.1016/j.cell.2023.11.021
ec_funded: 1
external_id:
  pmid:
  - '38128538'
file:
- access_level: open_access
  checksum: 06fd236a9ee0b46ccb05f44695bfc34b
  content_type: application/pdf
  creator: dernst
  date_created: 2024-01-22T13:41:41Z
  date_updated: 2024-01-22T13:41:41Z
  file_id: '14874'
  file_name: 2024_Cell_Kuhn.pdf
  file_size: 13194060
  relation: main_file
  success: 1
file_date_updated: 2024-01-22T13:41:41Z
has_accepted_license: '1'
intvolume: '       187'
issue: '1'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc/4.0/
month: '01'
oa: 1
oa_version: Published Version
page: 130-148.e17
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: 262EF96E-B435-11E9-9278-68D0E5697425
  call_identifier: FWF
  grant_number: P29988
  name: RNA-directed DNA methylation in plant development
publication: Cell
publication_identifier:
  eissn:
  - 1097-4172
  issn:
  - 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: RAF-like protein kinases mediate a deeply conserved, rapid auxin response
tmp:
  image: /images/cc_by_nc.png
  legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
  name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
  short: CC BY-NC (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 187
year: '2024'
...
---
_id: '14591'
abstract:
- lang: eng
  text: Clathrin-mediated endocytosis (CME) is vital for the regulation of plant growth
    and development by controlling plasma membrane protein composition and cargo uptake.
    CME relies on the precise recruitment of regulators for vesicle maturation and
    release. Homologues of components of mammalian vesicle scission are strong candidates
    to be part of the scissin machinery in plants, but the precise roles of these
    proteins in this process is not fully understood. Here, we characterised the roles
    of Plant Dynamin-Related Proteins 2 (DRP2s) and SH3-domain containing protein
    2 (SH3P2), the plant homologue to Dynamins’ recruiters, like Endophilin and Amphiphysin,
    in the CME by combining high-resolution imaging of endocytic events in vivo and
    characterisation of the purified proteins in vitro. Although DRP2s and SH3P2 arrive
    similarly late during CME and physically interact, genetic analysis of the Dsh3p1,2,3
    triple-mutant and complementation assays with non-SH3P2-interacting DRP2 variants
    suggests that SH3P2 does not directly recruit DRP2s to the site of endocytosis.
    These observations imply that despite the presence of many well-conserved endocytic
    components, plants have acquired a distinct mechanism for CME. One Sentence Summary
    In contrast to predictions based on mammalian systems, plant Dynamin-related proteins
    2 are recruited to the site of Clathrin-mediated endocytosis independently of
    BAR-SH3 proteins.
acknowledged_ssus:
- _id: EM-Fac
- _id: LifeSc
- _id: Bio
article_processing_charge: No
author:
- first_name: Nataliia
  full_name: Gnyliukh, Nataliia
  id: 390C1120-F248-11E8-B48F-1D18A9856A87
  last_name: Gnyliukh
  orcid: 0000-0002-2198-0509
- 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: Marie-Kristin
  full_name: Nagel, Marie-Kristin
  last_name: Nagel
- first_name: Aline
  full_name: Monzer, Aline
  id: 2DB5D88C-D7B3-11E9-B8FD-7907E6697425
  last_name: Monzer
- first_name: Annamaria
  full_name: Hlavata, Annamaria
  id: 36062FEC-F248-11E8-B48F-1D18A9856A87
  last_name: Hlavata
- first_name: Erika
  full_name: Isono, Erika
  last_name: Isono
- first_name: Martin
  full_name: Loose, Martin
  id: 462D4284-F248-11E8-B48F-1D18A9856A87
  last_name: Loose
  orcid: 0000-0001-7309-9724
- first_name: Jiří
  full_name: Friml, Jiří
  id: 4159519E-F248-11E8-B48F-1D18A9856A87
  last_name: Friml
  orcid: 0000-0002-8302-7596
citation:
  ama: Gnyliukh N, Johnson AJ, Nagel M-K, et al. Role of dynamin-related proteins
    2 and SH3P2 in clathrin-mediated endocytosis in plants. <i>bioRxiv</i>. doi:<a
    href="https://doi.org/10.1101/2023.10.09.561523">10.1101/2023.10.09.561523</a>
  apa: Gnyliukh, N., Johnson, A. J., Nagel, M.-K., Monzer, A., Hlavata, A., Isono,
    E., … Friml, J. (n.d.). Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated
    endocytosis in plants. <i>bioRxiv</i>. <a href="https://doi.org/10.1101/2023.10.09.561523">https://doi.org/10.1101/2023.10.09.561523</a>
  chicago: Gnyliukh, Nataliia, Alexander J Johnson, Marie-Kristin Nagel, Aline Monzer,
    Annamaria Hlavata, Erika Isono, Martin Loose, and Jiří Friml. “Role of Dynamin-Related
    Proteins 2 and SH3P2 in Clathrin-Mediated Endocytosis in Plants.” <i>BioRxiv</i>,
    n.d. <a href="https://doi.org/10.1101/2023.10.09.561523">https://doi.org/10.1101/2023.10.09.561523</a>.
  ieee: N. Gnyliukh <i>et al.</i>, “Role of dynamin-related proteins 2 and SH3P2 in
    clathrin-mediated endocytosis in plants,” <i>bioRxiv</i>. .
  ista: Gnyliukh N, Johnson AJ, Nagel M-K, Monzer A, Hlavata A, Isono E, Loose M,
    Friml J. Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis
    in plants. bioRxiv, <a href="https://doi.org/10.1101/2023.10.09.561523">10.1101/2023.10.09.561523</a>.
  mla: Gnyliukh, Nataliia, et al. “Role of Dynamin-Related Proteins 2 and SH3P2 in
    Clathrin-Mediated Endocytosis in Plants.” <i>BioRxiv</i>, doi:<a href="https://doi.org/10.1101/2023.10.09.561523">10.1101/2023.10.09.561523</a>.
  short: N. Gnyliukh, A.J. Johnson, M.-K. Nagel, A. Monzer, A. Hlavata, E. Isono,
    M. Loose, J. Friml, BioRxiv (n.d.).
date_created: 2023-11-22T10:17:49Z
date_published: 2023-10-10T00:00:00Z
date_updated: 2023-12-01T13:51:06Z
day: '10'
department:
- _id: JiFr
- _id: MaLo
- _id: CaBe
doi: 10.1101/2023.10.09.561523
ec_funded: 1
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://www.biorxiv.org/content/10.1101/2023.10.09.561523v2
month: '10'
oa: 1
oa_version: Preprint
project:
- _id: 2564DBCA-B435-11E9-9278-68D0E5697425
  call_identifier: H2020
  grant_number: '665385'
  name: International IST Doctoral Program
publication: bioRxiv
publication_status: submitted
related_material:
  record:
  - id: '14510'
    relation: dissertation_contains
    status: public
status: public
title: Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis
  in plants
type: preprint
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
year: '2023'
...
---
_id: '12291'
abstract:
- lang: eng
  text: The phytohormone auxin triggers transcriptional reprogramming through a well-characterized
    perception machinery in the nucleus. By contrast, mechanisms that underlie fast
    effects of auxin, such as the regulation of ion fluxes, rapid phosphorylation
    of proteins or auxin feedback on its transport, remain unclear1,2,3. Whether auxin-binding
    protein 1 (ABP1) is an auxin receptor has been a source of debate for decades1,4.
    Here we show that a fraction of Arabidopsis thaliana ABP1 is secreted and binds
    auxin specifically at an acidic pH that is typical of the apoplast. ABP1 and its
    plasma-membrane-localized partner, transmembrane kinase 1 (TMK1), are required
    for the auxin-induced ultrafast global phospho-response and for downstream processes
    that include the activation of H+-ATPase and accelerated cytoplasmic streaming.
    abp1 and tmk mutants cannot establish auxin-transporting channels and show defective
    auxin-induced vasculature formation and regeneration. An ABP1(M2X) variant that
    lacks the capacity to bind auxin is unable to complement these defects in abp1
    mutants. These data indicate that ABP1 is the auxin receptor for TMK1-based cell-surface
    signalling, which mediates the global phospho-response and auxin canalization.
acknowledged_ssus:
- _id: Bio
- _id: EM-Fac
- _id: LifeSc
acknowledgement: We acknowledge K. Kubiasová for excellent technical assistance, J.
  Neuhold, A. Lehner and A. Sedivy for technical assistance with protein production
  and purification at Vienna Biocenter Core Facilities; Creoptix for performing GCI;
  and the Bioimaging, Electron Microscopy and Life Science Facilities at ISTA, the
  Plant Sciences Core Facility of CEITEC Masaryk University, the Core Facility CELLIM
  (MEYS CR, LM2018129 Czech-BioImaging) and J. Sprakel for their assistance. J.F.
  is grateful to R. Napier for many insightful suggestions and support. We thank all
  past and present members of the Friml group for their support and for other contributions
  to this effort to clarify the controversial role of ABP1 over the past seven years.
  The project received funding from the European Research Council (ERC) under the
  European Union’s Horizon 2020 research and innovation program (grant agreement no.
  742985 to J.F. and 833867 to D.W.); the Austrian Science Fund (FWF; P29988 to J.F.);
  the Netherlands Organization for Scientific Research (NWO; VICI grant 865.14.001
  to D.W. and VENI grant VI.Veni.212.003 to A.K.); the Ministry of Education, Science
  and Technological Development of the Republic of Serbia (contract no. 451-03-68/2022-14/200053
  to B.D.Ž.); and the MEXT/JSPS KAKENHI to K.T. (20K06685) and T.K. (20H05687 and
  20H05910).
article_processing_charge: No
article_type: original
author:
- first_name: Jiří
  full_name: Friml, Jiří
  id: 4159519E-F248-11E8-B48F-1D18A9856A87
  last_name: Friml
  orcid: 0000-0002-8302-7596
- first_name: Michelle C
  full_name: Gallei, Michelle C
  id: 35A03822-F248-11E8-B48F-1D18A9856A87
  last_name: Gallei
  orcid: 0000-0003-1286-7368
- first_name: Zuzana
  full_name: Gelová, Zuzana
  id: 0AE74790-0E0B-11E9-ABC7-1ACFE5697425
  last_name: Gelová
  orcid: 0000-0003-4783-1752
- 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: Ewa
  full_name: Mazur, Ewa
  last_name: Mazur
- first_name: Aline
  full_name: Monzer, Aline
  id: 2DB5D88C-D7B3-11E9-B8FD-7907E6697425
  last_name: Monzer
- 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: Mark
  full_name: Roosjen, Mark
  last_name: Roosjen
- first_name: Inge
  full_name: Verstraeten, Inge
  id: 362BF7FE-F248-11E8-B48F-1D18A9856A87
  last_name: Verstraeten
  orcid: 0000-0001-7241-2328
- first_name: Branka D.
  full_name: Živanović, Branka D.
  last_name: Živanović
- first_name: Minxia
  full_name: Zou, Minxia
  id: 5c243f41-03f3-11ec-841c-96faf48a7ef9
  last_name: Zou
- first_name: Lukas
  full_name: Fiedler, Lukas
  id: 7c417475-8972-11ed-ae7b-8b674ca26986
  last_name: Fiedler
- first_name: Caterina
  full_name: Giannini, Caterina
  id: e3fdddd5-f6e0-11ea-865d-ca99ee6367f4
  last_name: Giannini
- first_name: Peter
  full_name: Grones, Peter
  last_name: Grones
- first_name: Mónika
  full_name: Hrtyan, Mónika
  id: 45A71A74-F248-11E8-B48F-1D18A9856A87
  last_name: Hrtyan
- first_name: Walter
  full_name: Kaufmann, Walter
  id: 3F99E422-F248-11E8-B48F-1D18A9856A87
  last_name: Kaufmann
  orcid: 0000-0001-9735-5315
- first_name: Andre
  full_name: Kuhn, Andre
  last_name: Kuhn
- first_name: Madhumitha
  full_name: Narasimhan, Madhumitha
  id: 44BF24D0-F248-11E8-B48F-1D18A9856A87
  last_name: Narasimhan
  orcid: 0000-0002-8600-0671
- first_name: Marek
  full_name: Randuch, Marek
  id: 6ac4636d-15b2-11ec-abd3-fb8df79972ae
  last_name: Randuch
- first_name: Nikola
  full_name: Rýdza, Nikola
  last_name: Rýdza
- first_name: Koji
  full_name: Takahashi, Koji
  last_name: Takahashi
- first_name: Shutang
  full_name: Tan, Shutang
  id: 2DE75584-F248-11E8-B48F-1D18A9856A87
  last_name: Tan
  orcid: 0000-0002-0471-8285
- first_name: Anastasiia
  full_name: Teplova, Anastasiia
  id: e3736151-106c-11ec-b916-c2558e2762c6
  last_name: Teplova
- first_name: Toshinori
  full_name: Kinoshita, Toshinori
  last_name: Kinoshita
- first_name: Dolf
  full_name: Weijers, Dolf
  last_name: Weijers
- first_name: Hana
  full_name: Rakusová, Hana
  last_name: Rakusová
citation:
  ama: Friml J, Gallei MC, Gelová Z, et al. ABP1–TMK auxin perception for global phosphorylation
    and auxin canalization. <i>Nature</i>. 2022;609(7927):575-581. doi:<a href="https://doi.org/10.1038/s41586-022-05187-x">10.1038/s41586-022-05187-x</a>
  apa: Friml, J., Gallei, M. C., Gelová, Z., Johnson, A. J., Mazur, E., Monzer, A.,
    … Rakusová, H. (2022). ABP1–TMK auxin perception for global phosphorylation and
    auxin canalization. <i>Nature</i>. Springer Nature. <a href="https://doi.org/10.1038/s41586-022-05187-x">https://doi.org/10.1038/s41586-022-05187-x</a>
  chicago: Friml, Jiří, Michelle C Gallei, Zuzana Gelová, Alexander J Johnson, Ewa
    Mazur, Aline Monzer, Lesia Rodriguez Solovey, et al. “ABP1–TMK Auxin Perception
    for Global Phosphorylation and Auxin Canalization.” <i>Nature</i>. Springer Nature,
    2022. <a href="https://doi.org/10.1038/s41586-022-05187-x">https://doi.org/10.1038/s41586-022-05187-x</a>.
  ieee: J. Friml <i>et al.</i>, “ABP1–TMK auxin perception for global phosphorylation
    and auxin canalization,” <i>Nature</i>, vol. 609, no. 7927. Springer Nature, pp.
    575–581, 2022.
  ista: Friml J, Gallei MC, Gelová Z, Johnson AJ, Mazur E, Monzer A, Rodriguez Solovey
    L, Roosjen M, Verstraeten I, Živanović BD, Zou M, Fiedler L, Giannini C, Grones
    P, Hrtyan M, Kaufmann W, Kuhn A, Narasimhan M, Randuch M, Rýdza N, Takahashi K,
    Tan S, Teplova A, Kinoshita T, Weijers D, Rakusová H. 2022. ABP1–TMK auxin perception
    for global phosphorylation and auxin canalization. Nature. 609(7927), 575–581.
  mla: Friml, Jiří, et al. “ABP1–TMK Auxin Perception for Global Phosphorylation and
    Auxin Canalization.” <i>Nature</i>, vol. 609, no. 7927, Springer Nature, 2022,
    pp. 575–81, doi:<a href="https://doi.org/10.1038/s41586-022-05187-x">10.1038/s41586-022-05187-x</a>.
  short: J. Friml, M.C. Gallei, Z. Gelová, A.J. Johnson, E. Mazur, A. Monzer, L. Rodriguez
    Solovey, M. Roosjen, I. Verstraeten, B.D. Živanović, M. Zou, L. Fiedler, C. Giannini,
    P. Grones, M. Hrtyan, W. Kaufmann, A. Kuhn, M. Narasimhan, M. Randuch, N. Rýdza,
    K. Takahashi, S. Tan, A. Teplova, T. Kinoshita, D. Weijers, H. Rakusová, Nature
    609 (2022) 575–581.
date_created: 2023-01-16T10:04:48Z
date_published: 2022-09-15T00:00:00Z
date_updated: 2023-11-07T08:16:09Z
day: '15'
ddc:
- '580'
department:
- _id: JiFr
- _id: GradSch
- _id: EvBe
- _id: EM-Fac
doi: 10.1038/s41586-022-05187-x
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title: ABP1–TMK auxin perception for global phosphorylation and auxin canalization
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