title: Differential expression of active zone proteins in neuromuscular junctions suggests functional diversification.
abstract: Nerve terminals of the central nervous system (CNS) contain specialized release sites for synaptic vesicles, referred to as active zones. They are characterized by electron-dense structures that are tightly associated with the presynaptic plasma membrane and organize vesicle docking and priming sites. Recently, major protein constituents of active zones have been identified, including the proteins Piccolo, Bassoon, RIM, Munc13, ERCs/ELKs/CASTs and liprins. While it is becoming apparent that each of these proteins is essential for synaptic function in the CNS, it is not known to what extent these proteins are involved in synaptic function of the peripheral nervous system. Somatic neuromuscular junctions contain morphologically and functionally defined active zones with similarities to CNS synapses. In contrast, sympathetic neuromuscular varicosities lack active zone-like morphological specializations. Using immunocytochemistry at the light and electron microscopic level we have now performed a systematic investigation of all five major classes of active zone proteins in peripheral neuromuscular junctions. Our results show that somatic neuromuscular endplates contain a full complement of all active zone proteins. In contrast, varicosities of the vas deferens contain a subset of active zone proteins including Bassoon and ELKS2, with the other four components being absent. We conclude that Bassoon and ELKS2 perform independent and specialized functions in synaptic transmission of autonomic synapses.
authors.affiliation: Department of Neurobiology, MPI for Biophysical Chemistry, 37077 Göttingen/Germany.
authors.forename: Judyta
authors.initials: J
authors.lastname: Juranek
authors.forename: Konark
authors.initials: K
authors.lastname: Mukherjee
authors.forename: Michael
authors.initials: M
authors.lastname: Rickmann
authors.forename: Henrik
authors.initials: H
authors.lastname: Martens
authors.forename: Jaroslaw
authors.initials: J
authors.lastname: Calka
authors.forename: Thomas C
authors.initials: TC
authors.lastname: Südhof
authors.forename: Reinhard
authors.initials: R
authors.lastname: Jahn
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000378:metabolism; D000818:Animals; D003598:Cytoskeletal Proteins / Q000378:metabolism; D019204:GTP-Binding Proteins / Q000378:metabolism; D008297:Male; D008565:Membrane Proteins / Q000378:metabolism; D016253:Microscopy, Immunoelectron; D009046:Motor Neurons / Q000378:metabolism* / Q000648:ultrastructure; D018482:Muscle, Skeletal / Q000294:innervation / Q000648:ultrastructure; D009130:Muscle, Smooth / Q000294:innervation / Q000648:ultrastructure; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D009469:Neuromuscular Junction / Q000378:metabolism* / Q000648:ultrastructure; D009479:Neuropeptides / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D017779:Sympathetic Fibers, Postganglionic / Q000378:metabolism* / Q000648:ultrastructure; D013570:Synaptic Membranes / Q000378:metabolism* / Q000648:ultrastructure; D009435:Synaptic Transmission / Q000502:physiology*; D014446:Tyrosine 3-Monooxygenase / Q000378:metabolism
chemical_list: D048868:Adaptor Proteins, Signal Transducing; C113688:Bsn protein, rat; D003598:Cytoskeletal Proteins; C479909:ERC1 protein, rat; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D009479:Neuropeptides; C470384:PPFIA2 protein, human; C405514:Pclo protein, rat; C491489:Rims1 protein, rat; C103912:Unc13a protein, rat; D014446:Tyrosine 3-Monooxygenase; D019204:GTP-Binding Proteins