Dystroglycans are essential elements of the neuromuscular junction (NMJ). The gene for dystroglycan is expressed as a precursor protein that is post translationally cleaved into a 156 kDa extracellular peripheral membrane protein called alpha dystroglycan and a 43 kDa transmembrane protein, beta dystroglycan. The latter protein contains a PPxY motif that promotes binding to WW domain containing proteins, such as utrophin and dystrophin. Phosphorylation at tyrosine 892 within the PPxY motif may regulate c Src interactions with beta dystroglycan, as well as inhibit interactions with WW domain proteins. In skeletal muscle, beta dystroglycan is normally localized to the plasma membrane, however phosphorylation of Tyr892 leads to localization of beta dystroglycan to endosomal compartments along with c Src. Thus, phosphorylation at Tyr892 may have important roles in altering the localization of beta dystroglycan during NMJ formation.
We offer labeled antibodies using our catalogue antibody products and a broad range of intensely fluorescent dyes and labels including HRP, biotin, ALP, Alexa Fluor® dyes, DyLight® Fluor dyes, R-phycoerythrin (R-PE), at scales from less than 100 μg up to 1 g of IgG antibody. Learn More
Citations
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POMERANZ, HD; SHERMAN, DL; et al. EXPRESSION OF A NEURALLY RELATED LAMININ BINDING-PROTEIN BY NEURAL CREST-DERIVED CELLS THAT COLONIZE THE GUT - RELATIONSHIP TO THE FORMATION OF ENTERIC GANGLIA. JOURNAL OF COMPARATIVE NEUROLOGY 313:625-642(1991).
Weir, ML; Oppizzi, ML; et al. Dystroglycan loss disrupts polarity and beta-casein induction in mammary epithelial cells by perturbing laminin anchoring. JOURNAL OF CELL SCIENCE 119:4047-4058(2006).
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