Evidence map›Paper›PMID 20430885›Full record

ArticleThe Journal of biological chemistry2010

J domain co-chaperone specificity defines the role of BiP during protein translocation.

Shruthi S Vembar, Martin C Jonikas, Linda M Hendershot, Jonathan S Weissman, Jeffrey L Brodsky

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

25 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. RNA modification enzyme TruB is a tRNA chaperone.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. ERdj3 regulates BiP occupancy in living cells.Journal of cell science · 2013
    Article
  20. Hsp70 protein complexes as drug targets.Current pharmaceutical design · 2013
    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 3 institutions in 1 country.

Shruthi S VembarDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA.
Martin C Jonikas
Linda M Hendershot
Jonathan S Weissman
Jeffrey L Brodsky
QB3 · USUniversity of Pittsburgh · USSt. Jude Children's Research Hospital · US

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
Role of Molecular Chaperones in Ig Biosynthesis 11-2008R01GM054068 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI HENDERSHOT, LINDA M · 1996 to 2018
$5.7M
ER Associated Degradation of Membrane Proteins in YeastR01GM075061 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BRODSKY, JEFFREY L. · 2006 to 2019
$3.2M
Howard Hughes Medical InstituteNCI NIH HHS CA21765NCI NIH HHS P30 CA021765NIGMS NIH HHS GM54068NIGMS NIH HHS GM75061NIGMS NIH HHS R01 GM054068NIGMS NIH HHS R01 GM075061
6 · The paper itself

Abstract

Hsp70 chaperones can potentially interact with one of several J domain-containing Hsp40 co-chaperones to regulate distinct cellular processes. However, features within Hsp70s that determine Hsp40 specificity are undefined. To investigate this question, we introduced mutations into the ER-lumenal Hsp70, BiP/Kar2p, and found that an R217A substitution in the J domain-interacting surface of BiP compromised the physical and functional interaction with Sec63p, an Hsp40 required for ER translocation. In contrast, interaction with Jem1p, an Hsp40 required for ER-associated degradation, was unaffected. Moreover, yeast expressing R217A BiP exhibited defects in translocation but not in ER-associated degradation. Finally, the genetic interactions of the R217A BiP mutant were found to correlate with those of known translocation mutants. Together, our results indicate that residues within the Hsp70 J domain-interacting surface help confer Hsp40 specificity, in turn influencing distinct chaperone-mediated cellular activities.

Indexed as

Endoplasmic ReticulumFungal ProteinsHeat-Shock ProteinsHSP70 Heat-Shock ProteinsMembrane Transport ProteinsMolecular ChaperonesMutant ProteinsMutationProtein Processing, Post-TranslationalProtein Structure, SecondaryProtein Structure, TertiaryProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStress, PhysiologicalStructure-Activity RelationshipFungal ProteinsHeat-Shock ProteinsHSP70 Heat-Shock ProteinsKAR2 protein, yeastMembrane Transport ProteinsMolecular ChaperonesMutant ProteinsSaccharomyces cerevisiae ProteinsSEC63 protein, S cerevisiae

Identifiers

PMID20430885
PMCPMC2903355
OpenAlexW2128300600

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.