Syntaxin-1A modulates vesicle fusion in mammalian neurons via juxtamembrane domain dependent palmitoylation of its transmembrane domain.
juxtamembrane domain
mouse
neuroscience
neurotransmitter release
palmitoylation
syntaxin-1
syntaxin-3
transmembrane domain
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
31 05 2022
31 05 2022
Historique:
received:
25
02
2022
accepted:
30
05
2022
pubmed:
1
6
2022
medline:
14
6
2022
entrez:
31
5
2022
Statut:
epublish
Résumé
SNAREs are undoubtedly one of the core elements of synaptic transmission. Contrary to the well characterized function of their SNARE domains bringing the plasma and vesicular membranes together, the level of contribution of their juxtamembrane domain (JMD) and the transmembrane domain (TMD) to the vesicle fusion is still under debate. To elucidate this issue, we analyzed three groups of STX1A mutations in cultured mouse hippocampal neurons: (1) elongation of STX1A's JMD by three amino acid insertions in the junction of SNARE-JMD or JMD-TMD; (2) charge reversal mutations in STX1A's JMD; and (3) palmitoylation deficiency mutations in STX1A's TMD. We found that both JMD elongations and charge reversal mutations have position-dependent differential effects on Ca
Identifiants
pubmed: 35638903
doi: 10.7554/eLife.78182
pii: 78182
pmc: PMC9183232
doi:
pii:
Substances chimiques
SNARE Proteins
0
Syntaxin 1
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© 2022, Vardar et al.
Déclaration de conflit d'intérêts
GV, AS, SZ, TT, CR No competing interests declared
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