Evidence map›Paper›PMID 20864538›Full record

ArticleThe Journal of biological chemistry2010

BiP modulates the affinity of its co-chaperone ERj1 for ribosomes.

Julia Benedix, Patrick Lajoie, Himjyot Jaiswal, Carsten Burgard, Markus Greiner, Richard Zimmermann, Sabine Rospert, Erik L Snapp, Johanna Dudek

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 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.4field-weighted citation impact, top 36% 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

19 citing papers in PubMed, 29 citations in OpenAlex.

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  13. The enigmatic ATP supply of the endoplasmic reticulum.Biological reviews of the Cambridge Philosophical Society · 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

9 authors at 3 institutions in 2 countries.

Julia BenedixDepartment of Medical Biochemistry and Molecular Biology, Saarland University, 66421 Homburg, Germany.
Patrick Lajoie
Himjyot Jaiswal
Carsten Burgard
Markus Greiner
Richard Zimmermann
Sabine Rospert
Erik L Snapp
Johanna Dudek
Saarland University · DEAlbert Einstein College of Medicine · USUniversity of Freiburg · DE

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
DETECTING AND RESPONDING TO MISFOLDED PROTEIN BURDENS IN AGING CELLSR21AG032544 · NIA · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI SCHMIDT, MARION, SNAPP, ERIK L. · 2008 to 2009
$457k
Polycystic Liver Disease and ER Quality ControlR21DK074650 · NIDDK · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI SNAPP, ERIK L. · 2006 to 2007
$449k
NIA NIH HHS R21 AG032544NIDDK NIH HHS R21 DK074650NIDDK NIH HHS R21 DK074650-01NIGMS NIH HHS R01 GM086530
6 · The paper itself

Abstract

Ribosomes synthesizing secretory and membrane proteins are bound to the endoplasmic reticulum (ER) membrane and attach to ribosome-associated membrane proteins such as the Sec61 complex, which forms the protein-conducting channel in the membrane. The ER membrane-resident Hsp40 protein ERj1 was characterized as being able to recruit BiP to ribosomes in solution and to regulate protein synthesis in a BiP-dependent manner. Here, we show that ERj1 and Sec61 are associated with ribosomes at the ER of human cells and that the binding of ERj1 to ribosomes occurs with a binding constant in the picomolar range and is prevented by pretreatment of ribosomes with RNase. However, the affinity of ERj1 for ribosomes dramatically changes upon binding of BiP. This modulation by BiP may be responsible for the dual role of ERj1 at the ribosome, i.e. acting as a recruiting factor for BiP and regulating translation.

Indexed as

Protein BiosynthesisAnimalsChlorocebus aethiopsCOS CellsDNA-Binding ProteinsEndoplasmic ReticulumHep G2 CellsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHumansMicroscopy, FluorescenceMolecular ChaperonesOligopeptidesOncogene ProteinsRibosomesRNA-Binding ProteinsBax-inhibiting peptide, BIPDNA-Binding ProteinsDNAJC2 protein, humanHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMolecular ChaperonesOligopeptidesOncogene ProteinsRNA-Binding Proteins

Identifiers

PMID20864538
PMCPMC2978572
OpenAlexW2139675721

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.