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Article

ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load.

The Journal of cell biology - 6 Aug 2012

Chambers Joseph E, Petrova Kseniya, Tomba Giulia, Vendruscolo Michele, Ron David

Abstract excerpt

Gene expression programs that regulate the abundance of the chaperone BiP adapt the endoplasmic reticulum (ER) to unfolded protein load. However, such programs are slow compared with physiological fluctuations in secreted protein synthesis. While searching for mechanisms that fill this temporal gap in coping with ER stress, we found elevated levels of adenosine diphosphate (ADP)-ribosylated BiP in the inactive...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 22869598
DOI: 10.1083/jcb.201202005
PMCID: PMC3413365

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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