ArticleStructure (London, England : 1993)2015
A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 100 citations in OpenAlex.
- Domain-dependent uncoupling of the co-chaperone and E3 ubiquitin ligase CHIP underlies heterogeneity in spinocerebellar ataxia 48.The Journal of biological chemistry · 2026Article
- Mitochondrial respiration modulates Hsf1 activation and the heat shock response.bioRxiv : the preprint server for biology · 2026Article
- Crystal structures reveal phosphorylation-dependent disruption of the heat shock protein 70-CHIP interface: A compensatory G132N variant restores binding affinity.Cell stress & chaperones · 2026Article
- Metabolomics reveals the therapeutic efficacy of liposomal resvida in endometrial cancer through regulating autophagy-related gene expression.Cancer cell international · 2025Article
- Functional and structural analyses of UbcH5 mutants with enhanced binding to the E3 ubiquitin ligase CHIP.Biochemical and biophysical research communications · 2025Article
- CHIP/STUB1 suppresses the transcription and latent reactivation of HIV-1 via the TRAF6-NF-κB-HIV-LTR axis.PLoS pathogens · 2025Article
- Degradation of nNOS in the PVN of Rats With Heart Failure: Role of CHIP.Hypertension (Dallas, Tex. : 1979) · 2025Article
- Bioinformatics-based screening of genes associated with dilated cardiomyopathy.Journal of thoracic disease · 2025Article
- Advances in the structures, mechanisms and targeting of molecular chaperones.Signal transduction and targeted therapy · 2025Review
- Chaperone-dependent and chaperone-independent functions of carboxylate clamp tetratricopeptide repeat (CC-TPR) proteins.Trends in biochemical sciences · 2025Review
- Article
- The essential role of TTC28 in maintaining chromosomal stability via HSPA8 chaperone-mediated autophagy.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Targeting chaperone modifications: Innovative approaches to cancer treatment.The Journal of biological chemistry · 2024Review
- Phosphorylation of tau at a single residue inhibits binding to the E3 ubiquitin ligase, CHIP.Nature communications · 2024Article
- Mechanism and complex roles of HSC70/HSPA8 in viral entry.Virus research · 2024Review
- Proteostasis perturbation of N-Myc leveraging HSP70 mediated protein turnover improves treatment of neuroendocrine prostate cancer.Nature communications · 2024Article
- The ubiquitin codes in cellular stress responses.Protein & cell · 2024Review
- Real-time bio-layer interferometry ubiquitination assays as alternatives to western blotting.Analytical biochemistry · 2023Article
- Loss of regulation of protein synthesis and turnover underpins an attenuated stress response in senescent human mesenchymal stem cells.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Effect of evolution of the C-terminal region on chaperone activity of Hsp70.Protein science : a publication of the Protein Society · 2023Article
3 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 4 institutions in 1 country.
Funding
Abstract
The ubiquitin ligase CHIP plays an important role in cytosolic protein quality control by ubiquitinating proteins chaperoned by Hsp70/Hsc70 and Hsp90, thereby targeting such substrate proteins for degradation. We present a 2.91 Å resolution structure of the tetratricopeptide repeat (TPR) domain of CHIP in complex with the α-helical lid subdomain and unstructured tail of Hsc70. Surprisingly, the CHIP-TPR interacts with determinants within both the Hsc70-lid subdomain and the C-terminal PTIEEVD motif of the tail, exhibiting an atypical mode of interaction between chaperones and TPR domains. We demonstrate that the interaction between CHIP and the Hsc70-lid subdomain is required for proper ubiquitination of Hsp70/Hsc70 or Hsp70/Hsc70-bound substrate proteins. Posttranslational modifications of the Hsc70 lid and tail disrupt key contacts with the CHIP-TPR and may regulate CHIP-mediated ubiquitination. Our study shows how CHIP docks onto Hsp70/Hsc70 and defines a bipartite mode of interaction between TPR domains and their binding partners.
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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.