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Protein–lipid interplay at the neuromuscular junction

Microscopy, 2022-02, Vol.71 (Supplement_1), p.i66-i71 [Peer Reviewed Journal]

The Author(s) 2022. Published by Oxford University Press on behalf of The Japanese Society of Microscopy. 2022 ;The Author(s) 2022. Published by Oxford University Press on behalf of The Japanese Society of Microscopy. ;ISSN: 2050-5698 ;EISSN: 2050-5701 ;DOI: 10.1093/jmicro/dfab023 ;PMID: 34226930

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  • Title:
    Protein–lipid interplay at the neuromuscular junction
  • Author: Unwin, Nigel
  • Subjects: Special Issue Paper
  • Is Part Of: Microscopy, 2022-02, Vol.71 (Supplement_1), p.i66-i71
  • Description: Abstract Many new structures of membrane proteins have been determined over the last decade, yet the nature of protein–lipid interplay has received scant attention. The postsynaptic membrane of the neuromuscular junction and Torpedo electrocytes has a regular architecture, opening an opportunity to illuminate how proteins and lipids act together in a native membrane setting. Cryo electron microscopy (Cryo-EM) images show that cholesterol segregates preferentially around the constituent ion channel, the nicotinic acetylcholine receptor, interacting with specific sites in both leaflets of the bilayer. In addition to maintaining the transmembrane α-helical architecture, cholesterol forms microdomains – bridges of rigid sterol groups that link one channel to the next. This article discusses the whole protein–lipid organization of the cholinergic postsynaptic membrane, its physiological implications and how the observed details relate to our current concept of the membrane structure. I suggest that cooperative interactions, facilitated by the regular protein–lipid arrangement, help to spread channel activation into regions distant from the sites of neurotransmitter release, thereby enhancing the postsynaptic response.
  • Publisher: UK: Oxford University Press
  • Language: English
  • Identifier: ISSN: 2050-5698
    EISSN: 2050-5701
    DOI: 10.1093/jmicro/dfab023
    PMID: 34226930
  • Source: Alma/SFX Local Collection
    Open Access: Oxford University Press Open Journals
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