English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Zendy Plus

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Zendy Tools

Zendy Open

At the neuromuscular junction (NMJ), the nicotinic acetylcholine receptor(nAChR) self-associates to give rise to rapid muscle movement. While lipiddomains have maintained nAChR aggregates in-vitro, their specific roles innAChR clustering are currently unknown. In the present study, we carried outcoarse-grained molecular dynamics simulations (CG-MD) of 1-4 nAChR molecules intwo membrane environments: One mixture containing domain-forming, homoacidiclipids, and a second mixture consisting of heteroacidic lipids. Spontaneousdimerization of nAChRs was up to ten times more likely in domain-formingmembranes; however, the effect was not significant in four-protein systems,suggesting that lipid domains are less critical to nAChR oligomerization whenprotein concentration is higher. With regard to lipid preferences, nAChRsconsistently partitioned into liquid-disordered domains occupied by the omega-3($\omega$-3) fatty acid, Docosahexaenoic acid (DHA); enrichment of DHA boundarylipids increased with protein concentration, particularly in homoacidicmembranes. This result suggests dimer formation blocks access of saturatedchains and cholesterol, but not polyunsaturated chains, to boundary lipidsites.

Untangling direct and domain-mediated interactions between nicotinic acetylcholine receptors in DHA-rich membranes