Vesicle capture by membrane-bound Munc13-1 requires selfassembly into discrete clusters - Université Côte d'Azur Accéder directement au contenu
Article Dans Une Revue FEBS Letters Année : 2021

Vesicle capture by membrane-bound Munc13-1 requires selfassembly into discrete clusters

Résumé

Munc13-1 is a large banana-shaped soluble protein that is involved in the regulation of synaptic vesicle docking and fusion. Recent studies suggest that multiple copies of Munc13-1 form nanoassemblies in active zones of neurons. However, it is not known if such clustering of Munc13-1 is correlated with multivalent binding to synaptic vesicles or specific plasma membrane domains at docking sites in the active zone. The functional significance of putative Munc13-1 clustering is also unknown. Here we report that nano-clustering is an inherent property of Munc13-1, and is indeed required for vesicle binding to bilayers containing Munc13-1. Purified Munc13-1 protein reconstituted onto supported lipid bilayers assembled into clusters containing from 2 to ~20 copies as revealed by a combination of quantitative TIRF microscopy and step-wise photobleaching. Surprisingly, only clusters containing a minimum of 6 copies of Munc13-1 were capable of efficiently capturing and retaining small unilamellar vesicles. The C-terminal C 2 C domain of Munc13-1 is not required for Munc13-1 clustering, but is required for efficient vesicle capture. This capture is largely due to a combination of electrostatic and hydrophobic interactions between the C 2 C domain and the vesicle membrane.
Fichier principal
Vignette du fichier
Li et al. - Vesicle capture by membrane-bound Munc13-1 require.pdf (1.23 Mo) Télécharger le fichier
Origine : Fichiers produits par l'(les) auteur(s)

Dates et versions

hal-03297036 , version 1 (23-07-2021)

Identifiants

Citer

Feng Li, Venkat Kalyana Sundaram, Alberto T Gatta, Jeff Coleman, Sathish Ramakrishnan, et al.. Vesicle capture by membrane-bound Munc13-1 requires selfassembly into discrete clusters. FEBS Letters, 2021, 595 (17), pp.2185-2196. ⟨10.1002/1873-3468.14157⟩. ⟨hal-03297036⟩
75 Consultations
220 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More