ArticleMolecular and cellular biology2003
The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex.
Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers, 1 of them a synthesis that pooled it.
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Who cites it
83 citing papers in PubMed, 1 synthesis or guideline pooled it, 153 citations in OpenAlex.
- A meta-analysis of different von Hippel Lindau mutations: are they related to retinal capillary hemangioblastoma?Molecular genetics and genomics : MGG · 2022Pooled it
- Proteostasis and ageing dissidence.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- Integration of CCT/TRiC assembly, degradation and function: Chaperonin complexity in a cellular context.Cell stress & chaperones · 2026Review
- TRiC-assisted folding of class I HDAC family proteins regulated by distinct co-chaperone and cofactor networks.Science advances · 2026Article
- Protist oxygen-sensing and the role of prolyl hydroxylase-regulation of E3(SCF) ubiquitin ligases.Biochimica et biophysica acta. General subjects · 2026Review
- Chaperonin in health and disease.Molecular biomedicine · 2026Review
- DCAF12 Ubiquitin Ligase Promotes Lung Cancer Metastasis by Modulating the TRiC/CCT Chaperonin Complex.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Single-Step Purification of Endogenous Human Chaperonin CCT.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Scp160 deletion suppresses TDP-43 aggregation and toxicity inMicrobial cell (Graz, Austria) · 2026Article
- The TRiC/CCT Complex at the Crossroads of Metabolism and Hypoxia in GBM: Implications for IDH-Dependent Therapeutic Targeting.International journal of molecular sciences · 2025Review
- Glycoregulation of E3(SCF) ubiquitin ligases in unicellular eukaryotes.Glycobiology · 2025Review
- Dysregulation of the ubiquitin-proteasome system in von Hippel-Lindau syndrome: molecular insights and clinical perspectives.Clinical and experimental medicine · 2025Review
- Navigating the landscape of protein folding and proteostasis: from molecular chaperones to therapeutic innovations.Signal transduction and targeted therapy · 2025Review
- Review
- Targeting the mosquito prefoldin-chaperonin complex blocks Plasmodium transmission.Nature microbiology · 2025Article
- Review
- The recruitment of TRiC chaperonin in rotavirus viroplasms correlates with virus replication.mBio · 2024Article
- The structural basis of eukaryotic chaperonin TRiC/CCT: Action and folding.Molecules and cells · 2024Review
- Second international symposium on the chaperone code, 2023.Cell stress & chaperones · 2024Article
- Structural basis of plp2-mediated cytoskeletal protein folding by TRiC/CCT.Science advances · 2023Article
23 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The degree of cooperation and redundancy between different chaperones is an important problem in understanding how proteins fold in the cell. Here we use the yeast Saccharomyces cerevisiae as a model system to examine in vivo the chaperone requirements for assembly of the von Hippel-Lindau protein (VHL)-elongin BC (VBC) tumor suppressor complex. VHL and elongin BC expressed in yeast assembled into a correctly folded VBC complex that resembles the complex from mammalian cells. Unassembled VHL did not fold and remained associated with the cytosolic chaperones Hsp70 and TRiC/CCT, in agreement with results from mammalian cells. Analysis of the folding reaction in yeast strains carrying conditional chaperone mutants indicates that incorporation of VHL into VBC requires both functional TRiC and Hsp70. VBC assembly was defective in cells carrying either a temperature-sensitive ssa1 gene as their sole source of cytosolic Hsp70/SSA function or a temperature-sensitive mutation in CCT4, a subunit of the TRiC/CCT complex. Analysis of the VHL-chaperone interactions in these strains revealed that the cct4ts mutation decreased binding to TRiC but did not affect the interaction with Hsp70. In contrast, loss of Hsp70 function disrupted the interaction of VHL with both Hsp70 and TRiC. We conclude that, in vivo, folding of some polypeptides requires the cooperation of Hsp70 and TRiC and that Hsp70 acts to promote substrate binding to TRiC.
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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.