The dynamic interactome of human Aha1 upon Y223 phosphorylation

1Citations
Citations of this article
10Readers
Mendeley users who have this article in their library.

Abstract

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 PXD001737.

Cite

CITATION STYLE

APA

Wolfgeher, D., Dunn, D. M., Woodford, M. R., Bourboulia, D., Bratslavsky, G., Mollapour, M., … Truman, A. W. (2015). The dynamic interactome of human Aha1 upon Y223 phosphorylation. Data in Brief, 5, 752–755. https://doi.org/10.1016/j.dib.2015.10.028

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free