Threonine 22 phosphorylation attenuates Hsp90 interaction with co-chaperones and affects its chaperone activity

Heat Shock Protein 90 (Hsp90) is an essential molecular chaperone whose activity is regulated not only by co-chaperones but also by distinct post-translational modifications. We report here that casein kinase 2 phosphorylates a conserved threonine residue (T22) in α-helix 1 of the yeast Hsp90 N-doma...

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Main Authors: Mollapour, Mehdi, Tsutsumi, Shinji, Truman, Andrew W., Xu, Wanping, Vaughan, Cara K., Beebe, Kristin, Konstantinova, Anna, Vourganti, Srinivas, Panaretou, Barry, Piper, Peter W., Trepel, Jane B., Prodromou, Chrisostomos, Pearl, Laurence H., Neckers, Len
Format: Artigo
Language:Inglês
Published: 2011
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Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC3062913/
https://ncbi.nlm.nih.gov/pubmed/21419342
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.molcel.2011.02.011
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