Nitration Of Hsp90 On Tyrosine 33 Regulates Mitochondrial Metabolism

Creator

Maria C. Franco, University of Central Florida
Karina C. Ricart, The University of Alabama at Birmingham
Analía S. Gonzalez, Universidad de Buenos Aires
Cassandra N. Dennys, University of Central Florida
Pascal A. Nelson, University of Central Florida

Abstract

Background: Heat shock protein 90 (Hsp90) is a pro-survival molecular chaperone that is nitrated only in pathological conditions. Results: Hsp90 nitrated on tyrosine 33 down-regulates mitochondrial activity. Conclusion: Differential nitration states of Hsp90 regulate distinct aspects of cellular metabolism. Significance: This is the first demonstration of a site-specific-nitrated protein regulating mitochondrial metabolism.

Publication Date

7-31-2015

Publication Title

Journal of Biological Chemistry

Volume

290

Issue

31

Number of Pages

19055-19066

Document Type

Article

Personal Identifier

scopus

DOI Link

https://doi.org/10.1074/jbc.M115.663278

Copyright Status

Unknown

Socpus ID

84940558811 (Scopus)

Source API URL

https://api.elsevier.com/content/abstract/scopus_id/84940558811

STARS Citation

Franco, Maria C.; Ricart, Karina C.; Gonzalez, Analía S.; Dennys, Cassandra N.; and Nelson, Pascal A., "Nitration Of Hsp90 On Tyrosine 33 Regulates Mitochondrial Metabolism" (2015). Scopus Export 2015-2019. 475.
https://stars.library.ucf.edu/scopus2015/475