Identification of disufide bond formation between MitoNEET and Glutamate dehydrogenase 1.

Authors

Morgan Roberts, Eastern Illinois University
Jacquelyn Crail, Eastern Illinois University
Megan Laffoon, Eastern Illinois University
William Fernandez, Eastern Illinois University
Michael Menze, University of LouisvilleFollow
Mary Konkle, Eastern Illinois University

Document Type

Article

Publication Date

12-1-2013

Department

Biology

Abstract

MitoNEET is a protein that was identified as a drug target for diabetes, but its cellular function as well as its role in diabetes remains elusive. Protein pull-down experiments identified glutamate dehydrogenase 1 (GDH1) as a potential binding partner. GDH1 is a key metabolic enzyme with emerging roles in insulin regulation. MitoNEET forms a covalent complex with GDH1 through disulfide bond formation and acts as an activator. Proteomic analysis identified the specific cysteine residues that participate in the disulfide bond. This is the first report that effectively links mitoNEET to activation of the insulin regulator GDH1.

Comments

This article is also available at http://pubs.acs.org/doi/pdf/10.1021/bi401038w doi: 10.1021/bi401038w

ThinkIR Citation

Roberts, Morgan; Crail, Jacquelyn; Laffoon, Megan; Fernandez, William; Menze, Michael; and Konkle, Mary, "Identification of disufide bond formation between MitoNEET and Glutamate dehydrogenase 1." (2013). Faculty Scholarship. 110.
https://ir.library.louisville.edu/faculty/110