HSP90B-CDC37 chaperone complex

ComplexAc: CPX-3287

Mus musculus; 10090

Curated by:

IntAct

Components

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ComplexViewer 2.2.4by Rappsilber LaboratoryCdc37Hsp90ab1Cdc37Hsp90ab1tooltip
Legend Description Stoichiometry
protein - Cdc37 (unspecified role)
Hsp90 co-chaperone Cdc37
protein - Hsp90ab1 (unspecified role)
Heat shock protein HSP 90-beta

Function

A protein kinase chaperone complex required for the proper folding, maturation and stabilization of target proteins (mostly signalling protein kinases, some steroid hormone receptors), usually during or immediately after completion of translation. The highly conserved, phosphorylated CDC37-Ser13 is essential for complex assembly and target protein binding. CDC37-Ser13 is phosphorylated by Casein kinase II (CK2), which in turn is a target of CDC37 creating a positive feedback loop. CDC37-Ser13 is de-phosphorylated by PP5 (P53041). Target proteins are recognised by the CDC37 subunit. HSP90 does not bind any particular motif but rather associates with intrinsically unstable kinases. Complex binding also prevents rapid ubiquitin-dependent proteosomal degradation of target proteins.

Properties

CDC37 binds its target proteins via its N-terminus (1-121 aa, InterPro IPR013855) and the HSP90 subunit via its central domain. Binding of CDC37 to HSP90 blocks the ATP binding site on HSP90.

Assembly

Heterotetramer

Expression and Cellular Location

Gene Expression Map

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GO - Cellular Component (1)

HSP90-CDC37 chaperone complex

Additional Information

Further Reading

Identifier Title Author(s)
18359116 L347P PINK1 mutant that fails to bind to Hsp90/Cdc37 chaperones is rapidly degraded in a proteasome-dependent manner. Moriwaki Y, Kim YJ, Ido Y, Misawa H, Kawashima K, Endo S, Takahashi R.
19387550 Protein kinase CK2 in health and disease: CK2: the kinase controlling the Hsp90 chaperone machinery. Miyata Y.

Systematic Name

2xCdc37:2xHsp90ab1