Evidence map›Paper›PMID 16982678›Full record

ArticleMolecular and cellular biology2006

Polysome-bound endonuclease PMR1 is targeted to stress granules via stress-specific binding to TIA-1.

Feng Yang, Yong Peng, Elizabeth L Murray, Yuichi Otsuka, Nancy Kedersha, Daniel R Schoenberg

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

21 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
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  4. Ultra-deep sequencing of ribosome-associated poly-adenylated RNA in early Drosophila embryos reveals hundreds of conserved translated sORFs.DNA research : an international journal for rapid publication of reports on genes and genomes · 2016
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  14. Article
  15. Article
  16. Regulation of translation by stress granules and processing bodies.Progress in molecular biology and translational science · 2009
    Review
  17. Article
  18. Article
  19. Article
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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

6 authors at 2 institutions in 1 country.

Feng YangDepartment of Molecular and Cellular Biochemistry, The Ohio State University, 1645 Neil Avenue, Columbus, OH 43210-1218, USA.
Yong Peng
Elizabeth L Murray
Yuichi Otsuka
Nancy Kedersha
Daniel R Schoenberg
The Ohio State University · USBrigham and Women's Hospital · US

Funding

Translational Therapeutics Research Program (TT)P30CA016058 · NCI · OHIO STATE UNIVERSITY · PI Tasleem J Padamsee · 1985 to 2026
$132.3M
Hormonal Regulation of mRNA StabilityR01GM038277 · NIGMS · OHIO STATE UNIVERSITY · PI SCHOENBERG, DANIEL R. · 1987 to 2013
$4.8M
CYTOLYTIC EFFECTOR MECHANISMS OF NUCLEOLYSIN TIA-1R01AI033600 · NIAID · DANA-FARBER CANCER INSTITUTE · PI ANDERSON, PAUL J. · 1993 to 2010
$3.4M
Characterization of mammalian stress granulesR56AI033600 · NIAID · BRIGHAM AND WOMEN'S HOSPITAL · PI ANDERSON, PAUL J. · 2005 to 2005
$437k
NCI NIH HHS P30 CA016058NCI NIH HHS P30 CA 16058NIAID NIH HHS AI 33600NIAID NIH HHS R01 AI033600NIAID NIH HHS R56 AI033600NIGMS NIH HHS GM 38277NIGMS NIH HHS R01 GM038277
6 · The paper itself

Abstract

The generalized process of mRNA decay involves deadenylation followed by release from translating polysomes, decapping, and exonuclease decay of the mRNA body. In contrast the mRNA endonuclease PMR1 forms a selective complex with its translating substrate mRNA, where it initiates decay by cleaving within the mRNA body. In stressed cells the phosphorylation of the alpha subunit of eukaryotic initiation factor 2 causes translating mRNAs to accumulate with stalled 48S subunits in large subcellular structures termed stress granules (SGs), wherein mRNAs undergo sorting for reinitiation, storage, or decay. Given the unique relationship between translation and PMR1-mediated mRNA decay, we examined the impact of stress-induced dissociation of polysomes on this process. Arsenite stress disrupts the polysome binding of PMR1 and its substrate mRNA but has no impact on the critical tyrosine phosphorylation of PMR1, its association with substrate mRNA, or its association with the functional approximately 680-kDa mRNP complex in which it normally resides on polysomes. We show that arsenite stress drives PMR1 into an RNase-resistant complex with TIA-1, and we identify a distinct domain in the N terminus of PMR1 that facilitates its interaction with TIA-1. Finally, we show that arsenite promotes the delayed association of PMR1 with SGs under conditions which cause tristetraprolin and butyrate response factor 1, proteins that facilitate exonucleolytic mRNA, to exit SGs.

Indexed as

AnimalsChlorocebus aethiopsCOS CellsCytoplasmic GranulesEndoribonucleasesGreen Fluorescent ProteinsMembrane ProteinsPoly(A)-Binding ProteinsPolyribosomesProtein BindingRecombinant Fusion ProteinsStress, PhysiologicalT-Cell Intracellular Antigen-1TransfectionEndoribonucleasesGreen Fluorescent ProteinsMembrane ProteinsPoly(A)-Binding Proteinspolysomal RNase 1Recombinant Fusion ProteinsT-Cell Intracellular Antigen-1TIA1 protein, human

Identifiers

PMID16982678
PMCPMC1636822
OpenAlexW2117633124

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.