DYNAMIC TYROSINE PHOSPHORYLATION MODULATES CYCLING OF THE HSP90-P50(CDC37)-AHA1 CHAPERONE MACHINE

Many critical protein kinases rely on the Hsp90 chaperone machinery for stability and function. After initially forming a ternary complex with kinase client and the co-chaperone p50(Cdc37), Hsp90 proceeds through a cycle of conformational changes facilitated by ATP binding and hydrolysis. Progressio...

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Main Authors: Xu, Wanping, Mollapour, Mehdi, Prodromou, Chrisostomos, Wang, Suiquan, Scroggins, Bradley T, Palchick, Zach, Beebe, Kristin, Siderius, Marco, Lee, Min-Jung, Couvillon, Anthony, Trepel, Jane B, Miyata, Yoshihiko, Matts, Robert, Neckers, Len
Formato: Artigo
Idioma:Inglês
Publicado: 2012
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Article
Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC3418412/
https://ncbi.nlm.nih.gov/pubmed/22727666
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.molcel.2012.05.015
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