Membrane fusion by VAMP3 and plasma membrane t-SNAREs

Journal Article · Mon Sep 10 04:00:00 EDT 2007 · Experimental Cell Research

OSTI ID:21045886

Chuan, Hu ^[1]; Hardee, Deborah ^[1]; Minnear, Fred ^[1]

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1. Department of Physiology and Pharmacology, West Virginia University Health Sciences Center, Morgantown, WV 26506 (United States)

Pairing of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins on vesicles (v-SNAREs) and SNARE proteins on target membranes (t-SNAREs) mediates intracellular membrane fusion. VAMP3/cellubrevin is a v-SNARE that resides in recycling endosomes and endosome-derived transport vesicles. VAMP3 has been implicated in recycling of transferrin receptors, secretion of {alpha}-granules in platelets, and membrane trafficking during cell migration. Using a cell fusion assay, we examined membrane fusion capacity of the ternary complexes formed by VAMP3 and plasma membrane t-SNAREs syntaxin1, syntaxin4, SNAP-23 and SNAP-25. VAMP3 forms fusogenic pairing with t-SNARE complexes syntaxin1/SNAP-25, syntaxin1/SNAP-23 and syntaxin4/SNAP-25, but not with syntaxin4/SNAP-23. Deletion of the N-terminal domain of syntaxin4 enhanced membrane fusion more than two fold, indicating that the N-terminal domain negatively regulates membrane fusion. Differential membrane fusion capacities of the ternary v-/t-SNARE complexes suggest that transport vesicles containing VAMP3 have distinct membrane fusion kinetics with domains of the plasma membrane that present different t-SNARE proteins.

• OSTI ID: 21045886
• Journal Information: Experimental Cell Research, Journal Name: Experimental Cell Research Journal Issue: 15 Vol. 313; ISSN 0014-4827; ISSN ECREAL
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
CELL CONSTITUENTS
CELL MEMBRANES
RECEPTORS
SECRETION
TRANSFERRIN