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Article

Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteins.

Oncogene - 2 Jan 2015

Smith J R, de Billy E, Hobbs S, Powers M, Prodromou C, Pearl L, Clarke P A, Workman P

Abstract excerpt

The HSP90 molecular chaperone plays a key role in the maturation, stability and activation of its clients, including many oncogenic proteins. Kinases are a substantial and important subset of clients requiring the key cochaperone CDC37. We sought an improved understanding of protein kinase chaperoning by CDC37 in cancer cells. CDC37 overexpression in human colon cancer cells increased CDK4 protein levels, which...

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Share to Chaperonins
Share to Colonic Neoplasms
Share to Cyclin-Dependent Kinase 4

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cyclin-Dependent Kinase 6

Share to HCT116 Cells

Share to HSP90 Heat-Shock Proteins

Share to Proto-Oncogene Proteins c-raf

Share to Receptor, ErbB-2

Source

Open in PubMed Open full text

Identifiers

PMID: 24292678
DOI: 10.1038/onc.2013.519
PMCID: PMC3984902

Genes

CDC37
CDK4
CDK6
ERBB2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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