Evidence map›Paper›PMID 10777498›Full record

ArticleThe Journal of biological chemistry2000

Interaction of murine BiP/GRP78 with the DnaJ homologue MTJ1.

M Chevalier, H Rhee, E C Elguindi, S Y Blond

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

41 citing papers in PubMed, 101 citations in OpenAlex.

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  14. The Hsp70-Chaperone Machines in Bacteria.Frontiers in molecular biosciences · 2021
    Review
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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

4 authors at 1 institution in 1 country.

M ChevalierDepartment of Medicinal Chemistry and Pharmacognosy, University of Illinois, Chicago, Illinois 60607-7173, USA.
H Rhee
E C Elguindi
S Y Blond
University of Illinois Chicago · US

Funding

GRP78/BIP AND ASSISTED PROTEIN FOLDINGR01GM058107 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI BLOND, SYLVIE Y · 1998 to 2002
$548k
NIGMS NIH HHS GM58107NIGMS NIH HHS R01 GM058107-02NIGMS NIH HHS R01 GM058107-03
6 · The paper itself

Abstract

The activity of Hsp70 proteins is regulated by accessory proteins, among which the most studied are the members of the DnaJ-like protein family. BiP/GRP78 chaperones the translocation and maturation of secreted and membrane proteins in the endoplasmic reticulum. No DnaJ-like partner has been described so far to regulate the function of mammalian BiP/GRP78. We show here that murine BiP/GRP78 interacts with the lumenal J domain of the murine transmembrane protein MTJ1 (J-MTJ1). J-MTJ1 stimulates the ATPase activity of BiP/GRP78 at stoichiometric concentrations. The C-terminal tail of BiP/GRP78 is not required for the interaction with J-MTJ1, leaving the function of this portion of the molecule still unclear. Physical interactions between J-MTJ1 and BiP/GRP78 are stable and can be abolished by a single histidine --> glutamine substitution in the highly conserved HPD motif shared by all DnaJ-like proteins. The J-MTJ1 fragment, but not the mutant J-MTJ1:H89Q fragment, stimulates the ATPase activity of Escherichia coli DnaK, although at a higher concentration than its genuine partner DnaJ. Full-length DnaJ does not stimulate BiP over the range of concentrations investigated. These results indicate that the J domain of MTJ1 is sufficient for its interaction with BiP/GRP78 and cannot be substituted by E. coli DnaJ.

Indexed as

Escherichia coli ProteinsAdenosine TriphosphatasesAmino Acid MotifsAmino Acid SequenceAnimalsCarrier ProteinsCell NucleusCircular DichroismDose-Response Relationship, DrugEndoplasmic Reticulum Chaperone BiPEnzyme ActivationHeat-Shock ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsKineticsMiceAdenosine TriphosphatasesCarrier ProteinsDnajc1 protein, mouseDnaJ protein, E colidnaK protein, E coliEndoplasmic Reticulum Chaperone BiPEscherichia coli ProteinsHeat-Shock ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHspa5 protein, mouseMolecular ChaperonesNeoplasm ProteinsPeptidesRecombinant Proteins

Identifiers

PMID10777498
PMCPMC1534116
OpenAlexW2109961906

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.