Evidence map›Paper›PMID 32743235›Full record

ArticlePlant direct2020

Control of translation during the unfolded protein response in maize seedlings: Life without PERKs.

Pulkit Kanodia, Paramasivan Vijayapalani, Renu Srivastava, Ran Bi, Peng Liu, W Allen Miller, Stephen H Howell

Open access · goldAbstract read
In one paragraph

Article in Plant direct, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

9 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Article
  3. Ribosome Profiling of Plants.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
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

7 authors at 1 institution in 1 country.

Pulkit KanodiaPlant Pathology and Microbiology Department Iowa State University Ames IA USA.ORCID https://orcid.org/0000-0001-7904-5129
Paramasivan VijayapalaniPlant Science Institute Iowa State University Ames IA USA.
Renu SrivastavaPlant Science Institute Iowa State University Ames IA USA.
Ran BiStatistics Department Iowa State University Ames IA USA.
Peng LiuPlant Science Institute Iowa State University Ames IA USA.
W Allen MillerPlant Pathology and Microbiology Department Iowa State University Ames IA USA.ORCID https://orcid.org/0000-0003-0603-2751
Stephen H HowellInterdepartmental Genetics and Genomics Major Iowa State University Ames IA USA.ORCID https://orcid.org/0000-0001-5863-2527
Iowa State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The accumulation of misfolded proteins in the endoplasmic reticulum (ER) defines a condition called ER stress that induces the unfolded protein response (UPR). The UPR in mammalian cells attenuates protein synthesis initiation, which prevents the piling up of misfolded proteins in the ER. Mammalian cells rely on Protein Kinase RNA-Like Endoplasmic Reticulum Kinase (PERK) phosphorylation of eIF2α to arrest protein synthesis, however, plants do not have a PERK homolog, so the question is whether plants control translation in response to ER stress. We compared changes in RNA levels in the transcriptome to the RNA levels protected by ribosomes and found a decline in translation efficiency, including many UPR genes, in response to ER stress. The decline in translation efficiency is due to the fact that many mRNAs are not loaded onto polyribosomes (polysomes) in proportion to their increase in total RNA, instead some of the transcripts accumulate in stress granules (SGs). The RNAs that populate SGs are not derived from the disassembly of polysomes because protein synthesis remains steady during stress. Thus, the surge in transcription of UPR genes in response to ER stress is accompanied by the formation of SGs, and the sequestration of mRNAs in SGs may serve to temporarily relieve the translation load during ER stress.

Indexed as

ER stressprotein synthesisribosome profilingribosome‐protected fragmentsstress granulestranslation efficiency

Identifiers

PMID32743235
PMCPMC7390965
OpenAlexW3047423100

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.