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Identification of Disufide Bond Formation between MitoNEET and Glutamate Dehydrogenase 1
Biochemistry (2013)
  • Morgan E. Roberts, Eastern Illinois University
  • Jacquelyn P. Crail, Eastern Illinois University
  • Megan M. Laffoon, Eastern Illinois University
  • William G. Fernandez, Eastern Illinois University
  • Michael A Menze, University of Louisville
  • Mary E. Konkle, Eastern Illinois University
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.
  • MitoNEET,
  • GDH1,
  • diabetes
Publication Date
December, 2013
Publisher Statement
This article is also available at doi: 10.1021/bi401038w
Citation Information
Morgan E. Roberts, Jacquelyn P. Crail, Megan M. Laffoon, William G. Fernandez, et al.. "Identification of Disufide Bond Formation between MitoNEET and Glutamate Dehydrogenase 1" Biochemistry Vol. Article ASAP (2013)
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