α - Neurexin multiplexes 1 Dystroglycan Binding to α −
نویسندگان
چکیده
Carsten Reissner, Johanna Stahn, Dorothee Breuer, Martin Klose, Gottfried Pohlentz, Michael Mormann, and Markus Missler From the Institute of Anatomy and Molecular Neurobiology, Westfälische Wilhelms-University, Vesaliusweg 2-4, 48149 Münster, Germany; Institute of Medical Physics and Biophysics, Westfälische Wilhelms-University Robert-Koch Strasse 31, 48149 Münster, Germany Cluster of Excellence EXC 1003, Cells in Motion, CiM, Münster, Germany;
منابع مشابه
Dystroglycan Binding to α-Neurexin Competes with Neurexophilin-1 and Neuroligin in the Brain*
α-Neurexins (α-Nrxn) are mostly presynaptic cell surface molecules essential for neurotransmission that are linked to neuro-developmental disorders as autism or schizophrenia. Several interaction partners of α-Nrxn are identified that depend on alternative splicing, including neuroligins (Nlgn) and dystroglycan (αDAG). The trans-synaptic complex with Nlgn1 was extensively characterized and show...
متن کاملLike-acetylglucosaminyltransferase (LARGE)-dependent modification of dystroglycan at Thr-317/319 is required for laminin binding and arenavirus infection.
α-dystroglycan is a highly O-glycosylated extracellular matrix receptor that is required for anchoring of the basement membrane to the cell surface and for the entry of Old World arenaviruses into cells. Like-acetylglucosaminyltransferase (LARGE) is a key molecule that binds to the N-terminal domain of α-dystroglycan and attaches ligand-binding moieties to phosphorylated O-mannose on α-dystrogl...
متن کاملLARGE Expression Augments the Glycosylation of Glycoproteins in Addition to α-Dystroglycan Conferring Laminin Binding
Mutations in genes encoding glycosyltransferases (and presumed glycosyltransferases) that affect glycosylation and extracellular matrix binding activity of α-dystroglycan (α-DG) cause congenital muscular dystrophies (CMDs) with central nervous system manifestations. Among the identified genes, LARGE is of particular interest because its overexpression rescues glycosylation defects of α-DG in mu...
متن کاملDystroglycan Adds More Sugars to the Midline Cocktail
In this issue of Neuron, Wright et al. (2012) identify two novel mediators of α-dystroglycan glycosylation in mouse and unravel a novel function of glycosylated dystroglycan in axon guidance by providing evidence for direct binding of α-DG to the midline chemorepellent Slit2.
متن کاملDifferential glycosylation of α-dystroglycan and proteins other than α-dystroglycan by like-glycosyltransferase.
Genetic defects in like-glycosyltransferase (LARGE) cause congenital muscular dystrophy with central nervous system manifestations. The underlying molecular pathomechanism is the hypoglycosylation of α-dystroglycan (α-DG), which is evidenced by diminished immunoreactivity to IIH6C4 and VIA4-1, antibodies that recognize carbohydrate epitopes. Previous studies indicate that LARGE participates in ...
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تاریخ انتشار 2014