Evidence map›Paper›PMID 9199165›Full record

ArticleThe Journal of cell biology1997

The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiae.

A K Corsi, R Schekman

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In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

60 citing papers in PubMed, 146 citations in OpenAlex.

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  4. Chaperone-mediated reflux of secretory proteins to the cytosol during endoplasmic reticulum stress.Proceedings of the National Academy of Sciences of the United States of America · 2019
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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

2 authors at 1 institution in 1 country.

A K CorsiDepartment of Molecular and Cell Biology, Howard Hughes Medical Institute, University of California, Berkeley, California 94720, USA.
R Schekman
University of California, Berkeley · US

Funding

MOLECULAR STUDIES OF EUKARYOTIC CELL SURFACE GROWTHR01GM026755 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI SCHEKMAN, RANDY W. · 1985 to 2005
$1.1M
NIGMS NIH HHS GM26755NIGMS NIH HHS R01 GM026755
6 · The paper itself

Abstract

We studied the molecular nature of the interaction between the integral membrane protein Sec63p and the lumenal Hsp70 BiP to elucidate their role in the process of precursor transit into the ER of Saccharomyces cerevisiae. A lumenal stretch of Sec63p with homology to the Escherichia coli protein DnaJ is the likely region of interface between Sec63p and BiP. This domain, purified as a fusion protein (63Jp) with glutathione S-transferase (GST), mediated a stable ATP-dependent binding interaction between 63Jp and BiP and stimulated the ATPase activity of BiP. The interaction was highly selective because only BiP was retained on immobilized 63Jp when detergent-solubilized microsomes were mixed with ATP and the fusion protein. GST alone was inactive in these assays. Additionally, a GST fusion containing a point mutation in the lumenal domain of Sec63p did not interact with BiP. Finally, we found that the soluble Sec63p lumenal domain inhibited efficient precursor import into proteoliposomes reconstituted so as to incorporate both BiP and the fusion protein. We conclude that the lumenal domain of Sec63p is sufficient to mediate enzymatic interaction with BiP and that this interaction positioned at the translocation apparatus or translocon at the lumenal face of the ER is vital for protein translocation into the ER.

Indexed as

Gene Expression Regulation, FungalHeat-Shock ProteinsMembrane Transport ProteinsSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesFungal ProteinsHSP70 Heat-Shock ProteinsMembrane ProteinsSaccharomyces cerevisiaeAdenosine TriphosphatasesFungal ProteinsHeat-Shock ProteinsHSP70 Heat-Shock ProteinsKAR2 protein, yeastMembrane ProteinsMembrane Transport ProteinsSaccharomyces cerevisiae ProteinsSEC63 protein, S cerevisiae

Identifiers

PMID9199165
PMCPMC2137819
OpenAlexW2106635066

What OpenQuestion holds

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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.