Article
Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37.
Molecular cell - 26 Sept 2008
Vaughan Cara K, Mollapour Mehdi, Smith Jennifer R, Truman Andrew, Hu Bin, Good Valerie M, Panaretou Barry, Neckers Len, Clarke Paul A, Workman Paul, Piper Peter W, Prodromou Chrisostomos, Pearl Laurence H
Abstract excerpt
Activation of protein kinase clients by the Hsp90 system is mediated by the cochaperone protein Cdc37. Cdc37 requires phosphorylation at Ser13, but little is known about the regulation of this essential posttranslational modification. We show that Ser13 of uncomplexed Cdc37 is phosphorylated in vivo, as well as in binary complex with a kinase (C-K), or in ternary complex with Hsp90 and kinase (H-C-K). Whereas...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.