Identification of disulfide bond formation between MitoNEET and glutamate dehydrogenase 1

Biochemistry. 2013 Dec 17;52(50):8969-71. doi: 10.1021/bi401038w. Epub 2013 Dec 4.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Disulfides / chemistry
  • Disulfides / metabolism*
  • Glutamate Dehydrogenase / chemistry
  • Glutamate Dehydrogenase / metabolism*
  • Hep G2 Cells
  • Humans
  • Iron-Binding Proteins / chemistry
  • Iron-Binding Proteins / metabolism*
  • Liver / chemistry
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • Mice
  • Mitochondrial Proteins / chemistry
  • Mitochondrial Proteins / metabolism*
  • Models, Molecular
  • Receptors, Glutamate / chemistry
  • Receptors, Glutamate / metabolism*

Substances

  • CISD1 protein, human
  • Disulfides
  • Iron-Binding Proteins
  • Membrane Proteins
  • Mitochondrial Proteins
  • Receptors, Glutamate
  • mitoNEET protein, mouse
  • GluD1 protein, mouse
  • Glutamate Dehydrogenase
  • GLUD1 protein, human