---
_id: '14776'
abstract:
- lang: eng
  text: Soluble chaperones residing in the endoplasmic reticulum (ER) play vitally
    important roles in folding and quality control of newly synthesized proteins that
    transiently pass through the ER en route to their final destinations. These soluble
    residents of the ER are themselves endowed with an ER retrieval signal that enables
    the cell to bring the escaped residents back from the Golgi. Here, by using purified
    proteins, we showed that Nicotiana tabacum phytaspase, a plant aspartate-specific
    protease, introduces two breaks at the C-terminus of the N. tabacum ER resident
    calreticulin-3. These cleavages resulted in removal of either a dipeptide or a
    hexapeptide from the C-terminus of calreticulin-3 encompassing part or all of
    the ER retrieval signal. Consistently, expression of the calreticulin-3 derivative
    mimicking the phytaspase cleavage product in Nicotiana benthamiana cells demonstrated
    loss of the ER accumulation of the protein. Notably, upon its escape from the
    ER, calreticulin-3 was further processed by an unknown protease(s) to generate
    the free N-terminal (N) domain of calreticulin-3, which was ultimately secreted
    into the apoplast. Our study thus identified a specific proteolytic enzyme capable
    of precise detachment of the ER retrieval signal from a plant ER resident protein,
    with implications for the further fate of the escaped resident.
acknowledgement: "We thank C.U.T. Hellen for critically reading the manuscript. The
  MALDI MS facility and CLSM became available to us in the framework of Moscow State
  University Development Programs PNG 5.13 and PNR 5.13.\r\nThis work was funded by
  the Russian Science Foundation, grant numbers 19-14-00010 and 22-14-00071."
article_number: '16527'
article_processing_charge: Yes
article_type: original
author:
- first_name: Anastasiia
  full_name: Teplova, Anastasiia
  id: e3736151-106c-11ec-b916-c2558e2762c6
  last_name: Teplova
- first_name: Artemii A.
  full_name: Pigidanov, Artemii A.
  last_name: Pigidanov
- first_name: Marina V.
  full_name: Serebryakova, Marina V.
  last_name: Serebryakova
- first_name: Sergei A.
  full_name: Golyshev, Sergei A.
  last_name: Golyshev
- first_name: Raisa A.
  full_name: Galiullina, Raisa A.
  last_name: Galiullina
- first_name: Nina V.
  full_name: Chichkova, Nina V.
  last_name: Chichkova
- first_name: Andrey B.
  full_name: Vartapetian, Andrey B.
  last_name: Vartapetian
citation:
  ama: Teplova A, Pigidanov AA, Serebryakova MV, et al. Phytaspase Is capable of detaching
    the endoplasmic reticulum retrieval signal from tobacco calreticulin-3. <i>International
    Journal of Molecular Sciences</i>. 2023;24(22). doi:<a href="https://doi.org/10.3390/ijms242216527">10.3390/ijms242216527</a>
  apa: Teplova, A., Pigidanov, A. A., Serebryakova, M. V., Golyshev, S. A., Galiullina,
    R. A., Chichkova, N. V., &#38; Vartapetian, A. B. (2023). Phytaspase Is capable
    of detaching the endoplasmic reticulum retrieval signal from tobacco calreticulin-3.
    <i>International Journal of Molecular Sciences</i>. MDPI. <a href="https://doi.org/10.3390/ijms242216527">https://doi.org/10.3390/ijms242216527</a>
  chicago: Teplova, Anastasiia, Artemii A. Pigidanov, Marina V. Serebryakova, Sergei
    A. Golyshev, Raisa A. Galiullina, Nina V. Chichkova, and Andrey B. Vartapetian.
    “Phytaspase Is Capable of Detaching the Endoplasmic Reticulum Retrieval Signal
    from Tobacco Calreticulin-3.” <i>International Journal of Molecular Sciences</i>.
    MDPI, 2023. <a href="https://doi.org/10.3390/ijms242216527">https://doi.org/10.3390/ijms242216527</a>.
  ieee: A. Teplova <i>et al.</i>, “Phytaspase Is capable of detaching the endoplasmic
    reticulum retrieval signal from tobacco calreticulin-3,” <i>International Journal
    of Molecular Sciences</i>, vol. 24, no. 22. MDPI, 2023.
  ista: Teplova A, Pigidanov AA, Serebryakova MV, Golyshev SA, Galiullina RA, Chichkova
    NV, Vartapetian AB. 2023. Phytaspase Is capable of detaching the endoplasmic reticulum
    retrieval signal from tobacco calreticulin-3. International Journal of Molecular
    Sciences. 24(22), 16527.
  mla: Teplova, Anastasiia, et al. “Phytaspase Is Capable of Detaching the Endoplasmic
    Reticulum Retrieval Signal from Tobacco Calreticulin-3.” <i>International Journal
    of Molecular Sciences</i>, vol. 24, no. 22, 16527, MDPI, 2023, doi:<a href="https://doi.org/10.3390/ijms242216527">10.3390/ijms242216527</a>.
  short: A. Teplova, A.A. Pigidanov, M.V. Serebryakova, S.A. Golyshev, R.A. Galiullina,
    N.V. Chichkova, A.B. Vartapetian, International Journal of Molecular Sciences
    24 (2023).
date_created: 2024-01-10T09:24:35Z
date_published: 2023-11-01T00:00:00Z
date_updated: 2024-01-10T13:41:10Z
day: '01'
ddc:
- '580'
department:
- _id: JiFr
doi: 10.3390/ijms242216527
external_id:
  isi:
  - '001113792600001'
  pmid:
  - '38003717'
file:
- access_level: open_access
  checksum: 4df7d206ba022b7f54eff1f0aec1659a
  content_type: application/pdf
  creator: dernst
  date_created: 2024-01-10T13:39:42Z
  date_updated: 2024-01-10T13:39:42Z
  file_id: '14791'
  file_name: 2023_IJMS_Teplova.pdf
  file_size: 2637784
  relation: main_file
  success: 1
file_date_updated: 2024-01-10T13:39:42Z
has_accepted_license: '1'
intvolume: '        24'
isi: 1
issue: '22'
keyword:
- Inorganic Chemistry
- Organic Chemistry
- Physical and Theoretical Chemistry
- Computer Science Applications
- Spectroscopy
- Molecular Biology
- General Medicine
- Catalysis
language:
- iso: eng
month: '11'
oa: 1
oa_version: Published Version
pmid: 1
publication: International Journal of Molecular Sciences
publication_identifier:
  issn:
  - 1422-0067
publication_status: published
publisher: MDPI
quality_controlled: '1'
status: public
title: Phytaspase Is capable of detaching the endoplasmic reticulum retrieval signal
  from tobacco calreticulin-3
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: 24
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
ec_funded: 1
external_id:
  isi:
  - '000851357500002'
  pmid:
  - '36071161'
file:
- access_level: open_access
  checksum: a6055c606aefb900bf62ae3e7d15f921
  content_type: application/pdf
  creator: amally
  date_created: 2023-11-02T17:12:37Z
  date_updated: 2023-11-02T17:12:37Z
  file_id: '14483'
  file_name: Friml Nature 2022_merged.pdf
  file_size: 79774945
  relation: main_file
  success: 1
file_date_updated: 2023-11-02T17:12:37Z
has_accepted_license: '1'
intvolume: '       609'
isi: 1
issue: '7927'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Submitted Version
page: 575-581
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: Nature
publication_identifier:
  eissn:
  - 1476-4687
  issn:
  - 0028-0836
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: ABP1–TMK auxin perception for global phosphorylation and auxin canalization
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 609
year: '2022'
...