Bmcc1s interacts with the phosphate-activated glutaminase in the brain

Biochimie. 2013 Apr;95(4):799-807. doi: 10.1016/j.biochi.2012.11.016. Epub 2012 Dec 12.

Abstract

Bmcc1s, a brain-enriched short isoform of the BCH-domain containing molecule Bmcc1, has recently been shown to interact with the microtubule-associated protein MAP6 and to regulate cell morphology. Here we identified kidney-type glutaminase (KGA), the mitochondrial enzyme responsible for the conversion of glutamine to glutamate in neurons, as a novel partner of Bmcc1s. Co-immunoprecipitation experiments confirmed that Bmcc1s and KGA form a physiological complex in the brain, whereas binding and modeling studies showed that they interact with each other. Overexpression of Bmcc1s in mouse primary cortical neurons impaired proper mitochondrial targeting of KGA leading to its accumulation within the cytoplasm. Thus, Bmcc1s may control the trafficking of KGA to the mitochondria.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Brain / cytology
  • Brain / metabolism*
  • Enzyme Activation / drug effects
  • Glutaminase / chemistry
  • Glutaminase / metabolism*
  • Humans
  • Kidney / enzymology
  • Mice
  • Mitochondria / drug effects
  • Mitochondria / metabolism
  • Models, Molecular
  • Neoplasm Proteins
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / metabolism*
  • Phosphates / pharmacology*
  • Protein Binding
  • Protein Conformation
  • Protein Transport / drug effects
  • Up-Regulation / drug effects

Substances

  • Neoplasm Proteins
  • Nerve Tissue Proteins
  • PRUNE2 protein, mouse
  • Phosphates
  • Glutaminase