Evidence map›Paper›PMID 23378021›Full record

ArticleJournal of cell science2013

ERdj3 regulates BiP occupancy in living cells.

Feng Guo, Erik L Snapp

Open access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

32 citing papers in PubMed, 53 citations in OpenAlex.

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  11. Comparative analysis of the coordinated motion of Hsp70s from different organelles observed by single-molecule three-color FRET.Proceedings of the National Academy of Sciences of the United States of America · 2021
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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.

Feng GuoDepartment of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Erik L Snapp
Albert Einstein College of Medicine · US

Funding

ER Chaperone Availability in Cells During Homeostasis and Misfolded Protein StresR01GM086530 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI SNAPP, ERIK L. · 2009 to 2010
$638k
NIGMS NIH HHS R01 GM086530NIGMS NIH HHS R01GM086530-01
6 · The paper itself

Abstract

Co-chaperones regulate chaperone activities and are likely to impact a protein-folding environment as much as the chaperone itself. As co-chaperones are expressed substoichiometrically, the ability of co-chaperones to encounter a chaperone is crucial for chaperone activity. ERdj3, an abundant soluble endoplasmic reticulum (ER) co-chaperone of the Hsp70 BiP, stimulates the ATPase activity of BiP to increase BiP's affinity for client (or substrate) proteins. We investigated ERdj3 availability, how ERdj3 levels impact BiP availability, and the significance of J proteins for regulating BiP binding of clients in living cells. FRAP analysis revealed that overexpressed ERdj3-sfGFP dramatically decreases BiP-GFP mobility in a client-dependent manner. By contrast, ERdj3-GFP mobility remains low regardless of client protein levels. Native gels and co-immunoprecipitations established that ERdj3 associates with a large complex including Sec61α. Translocon binding probably ensures rapid encounters between emerging nascent peptides and stimulates BiP activity in the crucial early stages of secretory protein folding. Importantly, mutant BiP exhibited significantly increased mobility when it could not interact with any ERdjs. Thus, ERdjs appear to play the dual roles of increasing BiP affinity for clients and regulating delivery of clients to BiP. Our data suggest that BiP engagement of clients is enhanced in ER subdomains enriched in ERdj proteins.

Indexed as

AnimalsCell Line, TumorDogsEndoplasmic ReticulumEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHSP40 Heat-Shock ProteinsHumansMadin Darby Canine Kidney CellsMembrane ProteinsMolecular ChaperonesMutationProtein BindingSEC Translocation ChannelsSubstrate SpecificityTransgenesDNAJB11 protein, humanEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHSP40 Heat-Shock ProteinsMembrane ProteinsMolecular ChaperonesSEC61A1 protein, humanSEC Translocation ChannelsBiPERdjFluorescence recovery after photobleachingFRAPQuality controlSuperfolder GFP

Identifiers

PMID23378021
PMCPMC3644143
OpenAlexW2166859880

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.