Cholinesterases and the basal lamina at vertebrate neuromuscular junctions.
Macromolecules of the cholinergic basal lamina are essential elements of the complex signaling processes governing development, function, and repair of the vertebrate neuromuscular junction. One special form of acetylcholinesterase (AChE) is anchored within BL through a collagen tail (ColQ) that binds heparan sulfate proteoglycans, such as perlecan, and the post-synaptic muscle specific kinase MuSK. New experimental approaches are probing the spatio-temporal dynamics of ColQ-AChE over days or weeks in vivo, thereby unraveling its interactions with other BL components, as well as pre-and post-synaptic elements. Concurrent advances in understanding of the biological effects of specific ColQ-AChE mutations prefigure improved diagnostics and clinical approaches for some congenital myasthenic syndromes.
Laboratoire de Neurobiologie, UMR8544 CNRS, Ecole Normale Supérieure, 46 rue d'Ulm, 75005 Paris, France. jean.massoulie@biologie.ens.fr
Jean
J
Massoulié
Charles B
CB
Millard
D000110:Acetylcholinesterase / Q000378:metabolism*; D000818:Animals; D001485:Basement Membrane / Q000201:enzymology*; D003094:Collagen / Q000378:metabolism; D019812:Heparan Sulfate Proteoglycans / Q000378:metabolism; D006801:Humans; D009124:Muscle Proteins / Q000378:metabolism; D009469:Neuromuscular Junction / Q000201:enzymology*; D020794:Receptor Protein-Tyrosine Kinases / Q000378:metabolism; D011950:Receptors, Cholinergic / Q000378:metabolism; D014714:Vertebrates
D019812:Heparan Sulfate Proteoglycans; D009124:Muscle Proteins; D011950:Receptors, Cholinergic; D003094:Collagen; C095714:MUSK protein, human; D020794:Receptor Protein-Tyrosine Kinases; D000110:Acetylcholinesterase; C114027:COLQ protein, human