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Identification of Disulfide Bond Formation between MitoNEET and Glutamate Dehydrogenase 1.

Authors :
Roberts, Morgan E.
Crail, Jacquelyn P.
Laffoon, Megan M.
Fernandez, William G.
Menze, Michael A.
Konkle, Mary E.
Source :
Biochemistry. 12/17/2013, Vol. 52 Issue 50, p8969-8971. 3p.
Publication Year :
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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00062960
Volume :
52
Issue :
50
Database :
Academic Search Index
Journal :
Biochemistry
Publication Type :
Academic Journal
Accession number :
93389367
Full Text :
https://doi.org/10.1021/bi401038w