Evidence map›Paper›PMID 11565755›Full record

ArticleRNA (New York, N.Y.)2001

Protein ligands mediate the CRM1-dependent export of HuR in response to heat shock.

I E Gallouzi, C M Brennan, J A Steitz

RetractedErratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

95 citing papers in PubMed, 165 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. RNA-Binding Proteins: Modulators of Canonical Wnt Signaling Pathway.International journal of molecular sciences · 2025
    Review
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  6. Article
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  8. Article
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  10. Elavl1 is dispensable for appendicular skeletal development.bioRxiv : the preprint server for biology · 2024
    Article
  11. Nuclear mRNA export.Acta biochimica et biophysica Sinica · 2024
    Review
  12. Article
  13. Article
  14. Relationship between HuR and tumor drug resistance.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2023
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 2 countries.

I E GallouziDepartment of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06536, USA.
C M Brennan
J A Steitz
Howard Hughes Medical Institute · USYale University · US

Funding

VIRAL SMALL RNPS--ROLES IN CELL TRANSFORMATIONP01CA016038 · NCI · YALE UNIVERSITY · PI DIMAIO, DANIEL C. · 1985 to 2020
$25.6M
NCI NIH HHS CA16038
6 · The paper itself

Abstract

AU-rich elements (AREs) located in the 3' UTRs of the messenger RNAs (mRNAs) of many mammalian early response genes promote rapid mRNA turnover. HuR, an RRM-containing RNA-binding protein, specifically interacts with AREs, stabilizing these mRNAs. HuR is primarily nucleoplasmic, but shuttles between the nucleus and the cytoplasm via a domain called HNS located between RRM2 and RRM3. We recently showed that HuR interacts with two protein ligands, pp32 and APRIL, which are also shuttling proteins, but rely on NES domains recognized by CRM1 for export. Here we show that heat shock induces increased association of HuR with pp32 and APRIL through protein-protein interactions and that these ligands partially colocalize with HuR in cytoplasmic foci. HuR associations with the hnRNP complex also increase, but through RNA links. CRM1 coimmunoprecipitates with HuR only after heat shock, and nuclear export of HuR becomes sensitive to leptomycin B, an inhibitor of CRM1. Export after heat shock requires the same domains of HuR (HNS and RRM3) that are essential for binding pp32 and APRIL. In situ hybridization and coimmunoprecipitation experiments show that LMB treatment blocks both hsp70 mRNA nuclear export and its cytoplasmic interaction with HuR after heat shock. Together, our results argue that upon heat shock, HuR switches its export pathway to that of its ligands pp32 and APRIL, which involves the nuclear export factor CRM1. HuR and its ligands may be instrumental in the nuclear export of heat-shock mRNAs.

Indexed as

Antigens, SurfaceHeat-Shock ResponseKaryopherinsReceptors, Cytoplasmic and NuclearActive Transport, Cell NucleusCarrier ProteinsCytoplasmELAV-Like Protein 1ELAV ProteinsExportin 1 ProteinFatty Acids, UnsaturatedHeLa CellsHumansLigandsNeuropeptidesNuclear ProteinsANP32B protein, humanAntigens, SurfaceCarrier ProteinsELAVL1 protein, humanELAV-Like Protein 1ELAV ProteinsExportin 1 ProteinFatty Acids, UnsaturatedKaryopherinsleptomycin BLigandsNeuropeptidesNuclear ProteinsPhosphoproteinsReceptors, Cytoplasmic and NuclearRNA-Binding ProteinsRNA, Messenger

Identifiers

PMID11565755
PMCPMC1370177
OpenAlexW2133590393

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.