Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 429, Issue 5, Pages 732-752Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2017.01.011
Keywords
molecular chaperone; Hsp90; post-translational modification; phosphorylation; evolution
Categories
Funding
- ZMBH Core Facility for Mass Spectrometry and Proteomics [SFB1036/Z1]
- ZMBH FACS Core Facility
- Deutsche Forschungsgemeinschaft [SFB638 A13, SFB/TRR77, SFB1036]
- National Natural Science Foundation of China [81171876]
Ask authors/readers for more resources
The 90-kDa heat shock proteins (Hsp90s) assist the maturation of many key regulators of signal transduction pathways and cellular control circuits like protein kinases and transcription factors and chaperone their stability and activity. In this function, Hsp90s cooperate with some 30 cochaperones and they are themselves subject to regulation by numerous post-translational modifications. In vertebrates, two major isoforms exist in the cytosol, Hsp90a and Hsp90p, which share a high degree of sequence identity and are expressed in tissue and environmental condition-dependent manner. We identified an isoform-specific phosphorylation site in human Hsp9013. This phosphorylation site seems to be linked to vertebrate evolution since it is not found in invertebrata but in all tetrapoda and many but not all fish species. We provide data suggesting that this phosphorylation is important for the activation of Hsp90 clients like glucocorticoid receptor and a protein kinase. Replacement of the phosphorylation site by glutamate affects the conformational dynamics of Hsp90 and interaction with the kinase-specific cochaperone Cdc37. (C) 2017 Elsevier Ltd. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available