2016
DOI: 10.1242/jcs.181180
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α-Dystrobrevin-1 recruits Grb2 and α-catulin to organize neurotransmitter receptors at the neuromuscular junction

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 dystrophinassociated 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-d… Show more

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Cited by 19 publications
(32 citation statements)
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“…Previous studies highlighted a critical role for the DGC in muscle fiber integrity and in the development of the postsynaptic machinery 6 . Using a biochemical screen, we recently identified liprin-α-1 as a binding partner for αDB1, a cytoplasmic component of the DGC 12 . Liprin-α-1 has not been reported at the vertebrate NMJ.…”
Section: Resultsmentioning
confidence: 99%
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“…Previous studies highlighted a critical role for the DGC in muscle fiber integrity and in the development of the postsynaptic machinery 6 . Using a biochemical screen, we recently identified liprin-α-1 as a binding partner for αDB1, a cytoplasmic component of the DGC 12 . Liprin-α-1 has not been reported at the vertebrate NMJ.…”
Section: Resultsmentioning
confidence: 99%
“…αDB1 binds to dystrophin, utrophin, and syntrophin and regulates the dynamics of AChR at the NMJ 11 – 14 . To gain further insights into the molecular function of αDB1, we recently performed a biochemical screen for αDB1-interacting partners and identified liprin-α-1 12 as one of these.…”
Section: Introductionmentioning
confidence: 99%
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“…The major difference between these two isoforms is the C‐terminal region present on α‐dystrobrevin‐1, which contains three phosphorylated tyrosines. These residues appear to be critical for at least some of the functions of α‐dystrobrevin‐1 at the NMJ, because their mutation significantly decreases the ability of mutant proteins to rescue the phenotypes of α‐dystrobrevin gene knockout mice …”
Section: Interactions Of Core Dgc Componentsmentioning
confidence: 99%
“…We recently performed biochemical studies that identified two groups of α‐dystrobrevin‐1–interacting proteins. The first group comprises proteins that bind α‐dystrobrevin‐1, regardless of its phosphorylation, including deubiquitinating enzyme USP9X and two scaffold proteins (α‐catulin and liprin‐α1) . The second group comprises proteins that are recruited to α‐dystrobrevin‐1 specifically upon its phosphorylation at Tyr713 and contains adaptor protein GRB2; phosphoinositide‐3 kinase (PI3K); the nonreceptor tyrosine‐protein kinases Fyn, Fer, and Hck; scaffold proteins SH3BP2 and SH2B; and Rho guanine nucleotide exchange factors ARHGEF2 and ARHGEF5 .…”
Section: Interactions Of Core Dgc Componentsmentioning
confidence: 99%