Evidence map›Paper›PMID 34618140›Full record

ArticlePlant physiology2021

OsFes1C, a potential nucleotide exchange factor for OsBiP1, is involved in the ER and salt stress responses.

Dandan Qian, Shuo Xiong, Mei Li, Lihong Tian, Le Qing Qu

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.0field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 28 citations in OpenAlex.

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  12. Editorial: Adaptive evolution of grasses.Frontiers in plant science · 2023
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  14. Distribution, expression of hexaploid wheatFrontiers in plant science · 2022
    Article
  15. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Dandan QianKey Laboratory of Plant Molecular Physiology, Institute of Botany, Innovation Academy for Seed Design, Chinese Academy of Sciences, Beijing 100093, China.
Shuo XiongKey Laboratory of Plant Molecular Physiology, Institute of Botany, Innovation Academy for Seed Design, Chinese Academy of Sciences, Beijing 100093, China.
Mei LiKey Laboratory of Plant Molecular Physiology, Institute of Botany, Innovation Academy for Seed Design, Chinese Academy of Sciences, Beijing 100093, China.ORCID 0000-0003-3052-9119
Lihong TianKey Laboratory of Plant Molecular Physiology, Institute of Botany, Innovation Academy for Seed Design, Chinese Academy of Sciences, Beijing 100093, China.ORCID 0000-0001-7435-3819
Le Qing QuKey Laboratory of Plant Molecular Physiology, Institute of Botany, Innovation Academy for Seed Design, Chinese Academy of Sciences, Beijing 100093, China.
Chinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The endoplasmic reticulum (ER) quality control system monitors protein homeostasis and relies on the activity of many molecular chaperones. Binding immunoglobulin protein (BiP) is a major ER luminal chaperone that is involved in most functions of the organelle. BiP activity is tightly regulated by nucleotide exchange factors (NEFs). However, information about NEFs in plants is limited. We obtained a Fes1-like protein (OsFes1C) through isobaric tags for relative and absolute quantitation-based proteomics analysis of ER-stressed rice (Oryza sativa) seeds. Unlike its homologs in yeast and mammals, which are located in the cytosol and respond to heat stress, OsFes1C is an ER membrane protein and responds to ER and salt stresses. OsFes1C interacts directly with OsBiP1 and the interaction is inhibited by ATP but promoted by ADP, suggesting that OsFes1C acts as a potential NEF of OsBiP1 in vivo. Overexpression or suppression of OsFes1C led to hypersensitivity to ER stress and affected the growth of rice. Furthermore, we established that OsFes1C directly interacts with a putative salt response protein and is involved in the salt response. Taken together, our study marks an important step toward elucidating the functional mechanisms of an identified ER stress response factor in rice.

Indexed as

Endoplasmic Reticulum StressMolecular ChaperonesOryzaPlant ProteinsSalt StressMolecular ChaperonesPlant Proteins

Identifiers

PMID34618140
PMCPMC8418431
OpenAlexW3166124822

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.