---
_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).
corr_author: '1'
date_created: 2024-01-10T09:24:35Z
date_published: 2023-11-01T00:00:00Z
date_updated: 2024-10-09T21:07:49Z
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
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  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
license: https://creativecommons.org/licenses/by/4.0/
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'
...
