Evidence map›Paper›PMID 10613902›Full record

ArticleThe Journal of cell biology1999

RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules.

N L Kedersha, M Gupta, W Li, I Miller, P Anderson

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 763 papers.

0numbers the graph read from it
0cells of the map it votes in
763citing papers in PubMed
3.2field-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

763 citing papers in PubMed, 1,262 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Prion-Like Protein LENG8-Mediated Nucleation Drives Stress Granule Assembly.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. TSC2 is a stress granule suppressor.bioRxiv : the preprint server for biology · 2026
    Article
  17. Article
  18. Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026
    Review
  19. Article
  20. Article

703 more citing papers are in PubMed but not listed here.

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.

N L KedershaDivision of Rheumatology and Immunology, Brigham and Women's Hospital, Smith Building, Boston, Massachusetts 02115, USA.
M Gupta
W Li
I Miller
P Anderson
Brigham and Women's Hospital · US

Funding

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
TNE ROLE OF TIAK IN APOPTOTIC CELL DEATHR01CA067929 · NCI · DANA-FARBER CANCER INSTITUTE · PI ANDERSON, PAUL J. · 1995 to 1999
–
NCI NIH HHS CA67929NIAID NIH HHS AI33600NIAID NIH HHS R01 AI033600NIAID NIH HHS R56 AI033600
6 · The paper itself

Abstract

In response to environmental stress, the related RNA-binding proteins TIA-1 and TIAR colocalize with poly(A)(+) RNA at cytoplasmic foci that resemble the stress granules (SGs) that harbor untranslated mRNAs in heat shocked plant cells (Nover et al. 1989; Nover et al. 1983; Scharf et al. 1998). The accumulation of untranslated mRNA at SGs is reversible in cells that recover from a sublethal stress, but irreversible in cells subjected to a lethal stress. We have found that the assembly of TIA-1/R(+) SGs is initiated by the phosphorylation of eIF-2alpha. A phosphomimetic eIF-2alpha mutant (S51D) induces the assembly of SGs, whereas a nonphosphorylatable eIF-2alpha mutant (S51A) prevents the assembly of SGs. The ability of a TIA-1 mutant lacking its RNA-binding domains to function as a transdominant inhibitor of SG formation suggests that this RNA-binding protein acts downstream of the phosphorylation of eIF-2alpha to promote the sequestration of untranslated mRNAs at SGs. The assembly and disassembly of SGs could regulate the duration of stress- induced translational arrest in cells recovering from environmental stress.

Indexed as

Heat-Shock ProteinsProteinsAnimalsCells, CulturedCOS CellsCytoplasmic GranulesEukaryotic Initiation Factor-2Hot TemperatureHSP27 Heat-Shock ProteinsHumansMaleMembrane ProteinsMolecular ChaperonesNeoplasm ProteinsPhosphorylationPoly(A)-Binding ProteinsEukaryotic Initiation Factor-2Heat-Shock ProteinsHSP27 Heat-Shock ProteinsHSPB1 protein, humanMembrane ProteinsMolecular ChaperonesNeoplasm ProteinsPoly(A)-Binding ProteinsProteinsRNA-Binding ProteinsT-Cell Intracellular Antigen-1TIA1 protein, humanTIAL1 protein, human

Identifiers

PMID10613902
PMCPMC2174242
OpenAlexW2138267133

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.