Bmcc1s interacts with the phosphate-activated glutaminase in the brain |
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| Authors: | Anne-Cé cile Boulay,Silvia Burbassi,Hans-Kristian Lorenzo,Damarys Loew,Pascal Ezan,Christian Giaume,Martine Cohen-Salmon |
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| Affiliation: | 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;2. University Pierre et Marie Curie, ED, No 158, 75005 Paris, France;3. MEMOLIFE Laboratory of Excellence and Paris Science Lettre Research University, 75005 Paris, France;4. Faculté de Medécine, Université Paris 11, Le Kremlin-Bicêtre, France;5. CHU Bicêtre, Service de Néphrologie, Le Kremlin-Bicêtre, France;6. INSERM U1014, Villejuif, France;g Institut Curie, Laboratory of Proteomic Mass Spectrometry, F-75248 Paris, France |
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| 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. |
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| Keywords: | Bmcc1 KGA Glutaminase Brain |
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