The dynamic interactome of human Aha1 upon Y223 phosphorylation
2015
Wolfgeher, Donald | Dunn, Diana M. | Woodford, Mark R. | Bourboulia, Dimitra | Bratslavsky, Gennady | Mollapour, Mehdi | Kron, Stephen J. | Truman, Andrew W.
Heat Shock Protein 90 (Hsp90) is an essential chaperone that supports the function of a wide range of signaling molecules. Hsp90 binds to a suite of co-chaperone proteins that regulate Hsp90 function through alteration of intrinsic ATPase activity. Several studies have determined Aha1 to be an important co-chaperone whose binding to Hsp90 is modulated by phosphorylation, acetylation and SUMOylation of Hsp90 [1,2]. In this study, we applied quantitative affinity-purification mass spectrometry (AP-MS) proteomics to understand how phosphorylation of hAha1 at Y223 altered global client/co-chaperone interaction [3]. Specifically, we characterized and compared the interactomes of Aha1–Y223F (phospho-mutant form) and Aha1–Y223E (phospho-mimic form). We identified 99 statistically significant interactors of hAha1, a high proportion of which (84%) demonstrated preferential binding to the phospho-mimic form of hAha1.The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository [4] with the dataset identifier http://www.ebi.ac.uk/pride/archive/projects/PXD001737.
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