ArticleThe Journal of biological chemistry2012
The DNAJA2 substrate release mechanism is essential for chaperone-mediated folding.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 53 citations in OpenAlex.
- Review
- CFTR Folding: From Structure and Proteostasis to Cystic Fibrosis Personalized Medicine.ACS chemical biology · 2023Review
- The self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70.Nature communications · 2023Article
- Data-driven large-scale genomic analysis reveals an intricate phylogenetic and functional landscape in J-domain proteins.Proceedings of the National Academy of Sciences of the United States of America · 2023Review
- J-domain protein chaperone circuits in proteostasis and disease.Trends in cell biology · 2023Review
- Identification of Sex-Specific Genetic Variants Associated With Tau PET.Neurology. Genetics · 2022Article
- An allosteric inhibitor of bacterial Hsp70 chaperone potentiates antibiotics and mitigates resistance.Cell chemical biology · 2022Article
- The chaperone HSPB1 prepares protein aggregates for resolubilization by HSP70.Scientific reports · 2021Article
- Ontogeny of hepatic metabolism in mule ducks highlights different gene expression profiles between carbohydrate and lipid metabolic pathways.BMC genomics · 2020Article
- Selective Binding of HSC70 and its Co-Chaperones to Structural Hotspots on CFTR.Scientific reports · 2020Article
- Broad-spectrum antitumor properties of Withaferin A: a proteomic perspective.RSC medicinal chemistry · 2020Review
- The Hsp70 chaperone network.Nature reviews. Molecular cell biology · 2019Review
- Hsp70 and DNAJA2 limit CFTR levels through degradation.PloS one · 2019Article
- Function, evolution, and structure of J-domain proteins.Cell stress & chaperones · 2019Article
- Genetic variation in N- and C-terminal regions of bovineJournal of genomics · 2018Article
- Chaperones rescue the energetic landscape of mutant CFTR at single molecule and in cell.Nature communications · 2017Article
- Bag1 Co-chaperone Promotes TRC8 E3 Ligase-dependent Degradation of Misfolded Human Ether a Go-Go-related Gene (hERG) Potassium Channels.The Journal of biological chemistry · 2017Article
- Hsp70/J-protein machinery from Glossina morsitans morsitans, vector of African trypanosomiasis.PloS one · 2017Article
- Reconstitution of a Mycobacterium tuberculosis proteostasis network highlights essential cofactor interactions with chaperone DnaK.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- ArHsp40, a type 1 J-domain protein, is developmentally regulated and stress inducible in post-diapause Artemia franciscana.Cell stress & chaperones · 2016Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
DNAJA1 (DJA1/Hdj2) and DNAJA2 (DJA2) are the major J domain partners of human Hsp70/Hsc70 chaperones. Although they have overall similarity with the well characterized type I co-chaperones from yeast and bacteria, they are biologically distinct, and their functional mechanisms are poorly characterized. We identified DJA2-specific activities in luciferase folding and repression of human ether-a-go-go-related gene (HERG) trafficking that depended on its expression levels in cells. Mutations in different internal domains of DJA2 abolished these effects. Using purified proteins, we addressed the mechanistic defects. A mutant lacking the region between the zinc finger motifs (DJA2-Δm2) was able to bind substrate similar to wild type but was incapable of releasing substrate during its transfer to Hsc70. The equivalent mutation in DJA1 also abolished its substrate release. A DJA2 mutant (DJA-221), which had its C-terminal dimerization region replaced by that of DJA1, was inactive but retained its ability to release substrate. The release mechanism required the J domain and ATP hydrolysis by Hsc70, although the nucleotide dependence diverged between DJA2 and DJA1. Limited proteolysis suggested further conformational differences between the two wild-type co-chaperones and the mutants. Our results demonstrate an essential role of specific DJA domains in the folding mechanism of Hsc70.
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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.