期刊
DATA IN BRIEF
卷 5, 期 -, 页码 752-755出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.dib.2015.10.028
关键词
Cancer; Hsp90; Interactome; Proteomics; Phosphorylation; Chaperones; Aha1; Co-chaperones
资金
- NCI [R01 CA164492]
- Deutsche Forschungsgemeinschaft [SFB638]
- Wellcome Trust [095605/Z11/Z]
- One Square Mile of Hope Foundation
- SUNY Upstate Medical University
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 Ahal 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 hAhal at Y223 altered global client/co-chaperone interaction [3]. Specifically, we characterized and compared the interactomes of Ahal-Y223F (phospho-mutant form) and Ahal-Y223E (phosphomimic form). We identified 99 statistically significant interactors of hAhal, a high proportion of which (84%) demonstrated preferential binding to the phospho-mimic form of hAhal. 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 PXD001737. (C) 2015 The Authors. Published by Elsevier Inc.
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