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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Huvudupphovsmän: 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
Materialtyp: Artigo
Språk:Inglês
Publicerad: 2014
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Article
Länkar: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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