Α-Dystrobrevin-1 recruits Grb2 and α-catulin to organize neurotransmitter receptors at the neuromuscular junction

Journal of Cell Science
Jacinthe GingrasTomasz J Proszynski

Abstract

Neuromuscular junctions (NMJs), the synapses made by motor neurons on muscle fibers, form during embryonic development but undergo substantial remodeling postnatally. Several lines of evidence suggest that α-dystrobrevin, a component of the dystrophin-associated glycoprotein complex (DGC), is a crucial regulator of the remodeling process and that tyrosine phosphorylation of one isoform, α-dystrobrevin-1, is required for its function at synapses. We identified a functionally important phosphorylation site on α-dystrobrevin-1, generated phosphorylation-specific antibodies to it and used them to demonstrate dramatic increases in phosphorylation during the remodeling period, as well as in nerve-dependent regulation in adults. We then identified proteins that bind to this site in a phosphorylation-dependent manner and others that bind to α-dystrobrevin-1 in a phosphorylation-independent manner. They include multiple members of the DGC, as well as α-catulin, liprin-α1, Usp9x, PI3K, Arhgef5 and Grb2. Finally, we show that two interactors, α-catulin (phosphorylation independent) and Grb2 (phosphorylation dependent) are localized to NMJs in vivo, and that they are required for proper organization of neurotransmitter receptors on myotubes.

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Citations

Oct 27, 2017·Annals of the New York Academy of Sciences·Marta Gawor, Tomasz J Prószyński
Dec 2, 2017·Annual Review of Physiology·Lei LiLin Mei
Feb 9, 2018·International Journal of Molecular Sciences·Steven J BurdenLeonor Remedio
Jun 27, 2020·Frontiers in Molecular Neuroscience·Krzysztof M BernadzkiPaweł Niewiadomski
Jun 14, 2020·The Journal of Biological Chemistry·Po-Ju ChenMohammed Akaaboune
Nov 25, 2020·International Journal of Molecular Sciences·Bhola Shankar Pradhan, Tomasz J Prószyński
Feb 15, 2020·Neuroscience Letters·Dina C Belhasan, Mohammed Akaaboune
Apr 20, 2021·Frontiers in Cell and Developmental Biology·Xingqiao XieZhiyi Wei

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