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Article

Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC.

Molecular cell - 1 Dec 1999

Feldman D E, Thulasiraman V, Ferreyra R G, Frydman J

Abstract excerpt

von Hippel-Lindau (VHL) disease is caused by loss of function of the VHL tumor suppressor protein. Here, we demonstrate that the folding and assembly of VHL into a complex with its partner proteins, elongin B and elongin C (herein, elongin BC), is directly mediated by the chaperonin TRiC/CCT. Association of VHL with TRiC is required for formation of the VHL-elongin BC complex. A 55-amino acid domain of VHL is...

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Source

Identifiers

PMID: 10635329
DOI: 10.1016/s1097-2765(00)80233-6

Genes

VHL

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC.PMID 10635329Read ↗

The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex.Semantic proximity Read ↗

Diverse effects of mutations in exon II of the von Hippel-Lindau (VHL) tumor suppressor gene on the interaction of pVHL with the cytosolic chaperonin and pVHL-dependent ubiquitin ligase activity.Semantic proximity Read ↗

Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function.Semantic proximity Read ↗

The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteinsSemantic proximity Read ↗

The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families.Semantic proximity Read ↗

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