The mesoscale organization of syntaxin 1A and SNAP25 is determined by SNARE-SNARE interactions.
biochemistry
cell biology
chemical biology
exocytosis
microdomains
plasma membrane
protein-nanoclustering
rat
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
15 11 2021
15 11 2021
Historique:
received:
08
04
2021
accepted:
14
11
2021
pubmed:
16
11
2021
medline:
15
12
2021
entrez:
15
11
2021
Statut:
epublish
Résumé
SNARE proteins have been described as the effectors of fusion events in the secretory pathway more than two decades ago. The strong interactions between SNARE domains are clearly important in membrane fusion, but it is unclear whether they are involved in any other cellular processes. Here, we analyzed two classical SNARE proteins, syntaxin 1A and SNAP25. Although they are supposed to be engaged in tight complexes, we surprisingly find them largely segregated in the plasma membrane. Syntaxin 1A only occupies a small fraction of the plasma membrane area. Yet, we find it is able to redistribute the far more abundant SNAP25 on the mesoscale by gathering crowds of SNAP25 molecules onto syntaxin clusters in a SNARE-domain-dependent manner. Our data suggest that SNARE domain interactions are not only involved in driving membrane fusion on the nanoscale, but also play an important role in controlling the general organization of proteins on the mesoscale. Further, we propose these mechanisms preserve active syntaxin 1A-SNAP25 complexes at the plasma membrane.
Identifiants
pubmed: 34779769
doi: 10.7554/eLife.69236
pii: 69236
pmc: PMC8629428
doi:
pii:
Substances chimiques
SNARE Proteins
0
Snap25 protein, rat
0
Stx1a protein, rat
0
Synaptosomal-Associated Protein 25
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
© 2021, Mertins et al.
Déclaration de conflit d'intérêts
JM, JF, RS, KR, JH, TL No competing interests declared
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