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Bmcc1s interacts with the phosphate-activated glutaminase in the brain.

Biochimie. 2013 Apr;95(4):799-807. Epub 2012 Dec 12
Anne-Cécile Boulay 1 , Silvia Burbassi , Hans-Kristian Lorenzo , Damarys Loew , Pascal Ezan , Christian Giaume , Martine Cohen-Salmon
Anne-Cécile Boulay 1 , Silvia Burbassi , Hans-Kristian Lorenzo , Damarys Loew , Pascal Ezan , Christian Giaume , Martine Cohen-Salmon
+ et al

[No authors listed]

Author information
  • 1 Collège de France, Center for Interdisciplinary Research in Biology (CIRB)/Centre National de la Recherche Scientifique, Unité Mixte de Recherche 7241/Institut National de la Santè et de la Recherche Médicale U1050, 11 Place Marcelin Berthelot, 75231 Paris Cedex 05, France.

摘要


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.