ArticleThe Journal of cell biology2012
ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load.
Article in The Journal of cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 54 papers.
What it found
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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.
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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.
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Who cites it
54 citing papers in PubMed, 98 citations in OpenAlex.
- The critical role of GRP78/BiP MARylation in ER stress of KRAS-mutant colorectal cancer.JCI insight · 2026Article
- GRP78 in human diseases: From molecular chaperone to therapeutic target.Theranostics · 2026Review
- FicD sensitizes cellular response to glucose fluctuations in mouse embryonic fibroblasts.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The Essential Functions of Molecular Chaperones and Folding Enzymes in Maintaining Endoplasmic Reticulum Homeostasis.Journal of molecular biology · 2024Review
- The interaction of GRP78 and Zika virus E and NS1 proteins occurs in a chaperone-client manner.Scientific reports · 2024Article
- Loss of Grp170 results in catastrophic disruption of endoplasmic reticulum function.Molecular biology of the cell · 2024Article
- Infancy-onset diabetes caused by de-regulated AMPylation of the human endoplasmic reticulum chaperone BiP.EMBO molecular medicine · 2023Article
- AMPylation and Endoplasmic Reticulum Protein Folding Homeostasis.Cold Spring Harbor perspectives in biology · 2023Review
- Article
- Fic-mediated AMPylation tempers the unfolded protein response during physiological stress.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Stress-induced protein disaggregation in the endoplasmic reticulum catalysed by BiP.Nature communications · 2022Article
- A novel and unique ATP hydrolysis to AMP by a human Hsp70 Binding immunoglobin protein (BiP).Protein science : a publication of the Protein Society · 2022Article
- Mitochondrial aspartate regulates TNF biogenesis and autoimmune tissue inflammation.Nature immunology · 2021Article
- Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD.Nature communications · 2021Article
- Identification of the role of mono-ADP-ribosylation in colorectal cancer by integrated transcriptome analysis.Medical oncology (Northwood, London, England) · 2021Article
- Kinetic and structural parameters governing Fic-mediated adenylylation/AMPylation of the Hsp70 chaperone, BiP/GRP78.Cell stress & chaperones · 2021Article
- On the Need to Tell Apart Fraternal Twins eEF1A1 and eEF1A2, and Their Respective Outfits.International journal of molecular sciences · 2021Review
- Co-occurrence of Protein Crotonylation and 2-Hydroxyisobutyrylation in the Proteome of End-Stage Renal Disease.ACS omega · 2021Article
- CBeLife · 2020Article
- Post-translational modifications of Hsp70 family proteins: Expanding the chaperone code.The Journal of biological chemistry · 2020Review
Corrections and comments
- Commented on by
- Erratum issued
Authors and funding
5 authors at 2 institutions in 3 countries.
Funding
Abstract
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 pancreas of fasted mice and a rapid decline in this modification in the active fed state. ADP ribosylation mapped to Arg470 and Arg492 in the substrate-binding domain of hamster BiP. Mutations that mimic the negative charge of ADP-ribose destabilized substrate binding and interfered with interdomain allosteric coupling, marking ADP ribosylation as a rapid posttranslational mechanism for reversible inactivation of BiP. A kinetic model showed that buffering fluctuations in unfolded protein load with a recruitable pool of inactive chaperone is an efficient strategy to minimize both aggregation and costly degradation of unfolded proteins.
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Registered trials
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.