Asymmetric Hsp90 N-domain SUMOylation recruits Aha1 and ATP-competitive inhibitors

The stability and activity of numerous signaling proteins in both normal and cancer cells depends on the dimeric molecular chaperone Heat Shock Protein 90 (Hsp90). Hsp90 function is coupled to ATP binding and hydrolysis, and requires a series of conformational changes that are regulated by co-chaper...

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Main Authors: Mollapour, Mehdi, Bourboulia, Dimitra, Beebe, Kristin, Woodford, Mark R., Polier, Sigrun, Hoang, Anthony, Chelluri, Raju, Li, Yu, Guo, Ailan, Lee, Min-Jung, Fotooh-Abadi, Elham, Khan, Sahar, Prince, Thomas, Miyajima, Naoto, Yoshida, Soichiro, Tsutsumi, Shinji, Xu, Wanping, Panaretou, Barry, Stetler-Stevenson, William G., Bratslavsky, Gennady, Trepel, Jane B., Prodromou, Chrisostomos, Neckers, Len
Formato: Artigo
Idioma:Inglês
Publicado: 2014
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Article
Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC3964875/
https://ncbi.nlm.nih.gov/pubmed/24462205
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.molcel.2013.12.007
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