Faculty Research & Creative Activity
Document Type
Article
Publication Date
December 2013
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.
Recommended Citation
Roberts, Morgan E.; Crail, Jacquelyn P.; Laffoon, Megan M.; Fernandez, William G.; Menze, Michael A.; and Konkle, Mary E., "Identification of Disulfide Bond Formation between MitoNEET and Glutamate Dehydrogenase 1" (2013). Faculty Research & Creative Activity. 235.
https://thekeep.eiu.edu/bio_fac/235
Comments
This article is also available at http://pubs.acs.org/doi/pdf/10.1021/bi401038w doi: 10.1021/bi401038w