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The structure of human neuromuscular junctions: some unanswered molecular questions

Lookup NU author(s): Emeritus Professor Clarke Slater

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This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


Abstract

The commands that control animal movement are transmitted from motor neurons totheir target muscle cells at the neuromuscular junctions (NMJs). The NMJs contain many proteinspecies whose role in transmission depends not only on their inherent properties, but also on howthey are distributed within the complex structure of the motor nerve terminal and the postsynapticmuscle membrane. These molecules mediate evoked chemical transmitter release from the nerveand the action of that transmitter on the muscle. Human NMJs are among the smallest known andrelease the smallest number of transmitter “quanta”. By contrast, they have the most deeply infoldedpostsynaptic membranes, which help to amplify transmitter action. The same structural features thatdistinguish human NMJs make them particularly susceptible to pathological processes. While muchhas been learned about the molecules which mediate transmitter release and action, little is knownabout the molecular processes that control the growth of the cellular and subcellular componentsof the NMJ so as to give rise to its mature form. A major challenge for molecular biologists is tounderstand the molecular basis for the development and maintenance of functionally importantaspects of NMJ structure, and thereby to point to new directions for treatment of diseases in whichneuromuscular transmission is impaired.


Publication metadata

Author(s): Slater CR

Publication type: Article

Publication status: Published

Journal: International Journal of Molecular Sciences

Year: 2017

Volume: 18

Issue: 10

Pages: 2183

Online publication date: 19/10/2017

Acceptance date: 13/10/2017

Date deposited: 22/11/2017

ISSN (print): 1661-6596

ISSN (electronic): 1422-0067

Publisher: MDPI

URL: https://doi.org/10.3390/ijms18102183

DOI: 10.3390/ijms18102183


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