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PMID:12145198
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| Citation |
Quetglas, S, Iborra, C, Sasakawa, N, De Haro, L, Kumakura, K, Sato, K, Leveque, C and Seagar, M (2002) Calmodulin and lipid binding to synaptobrevin regulates calcium-dependent exocytosis. EMBO J. 21:3970-9 |
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| Abstract |
Neurotransmitter release involves the assembly of a heterotrimeric SNARE complex composed of the vesicle protein synaptobrevin (VAMP 2) and two plasma membrane partners, syntaxin 1 and SNAP-25. Calcium influx is thought to control this process via Ca(2+)-binding proteins that associate with components of the SNARE complex. Ca(2+)/calmodulin or phospholipids bind in a mutually exclusive fashion to a C-terminal domain of VAMP (VAMP(77-90)), and residues involved were identified by plasmon resonance spectroscopy. Microinjection of wild-type VAMP(77-90), but not mutant peptides, inhibited catecholamine release from chromaffin cells monitored by carbon fibre amperometry. Pre-incubation of PC12 pheochromocytoma cells with the irreversible calmodulin antagonist ophiobolin A inhibited Ca(2+)-dependent human growth hormone release in a permeabilized cell assay. Treatment of permeabilized cells with tetanus toxin light chain (TeNT) also suppressed secretion. In the presence of TeNT, exocytosis was restored by transfection of TeNT-resistant (Q(76)V, F(77)W) VAMP, but additional targeted mutations in VAMP(77-90) abolished its ability to rescue release. The calmodulin- and phospholipid-binding domain of VAMP 2 is thus required for Ca(2+)-dependent exocytosis, possibly to regulate SNARE complex assembly. |
| Links |
PubMed PMC126150 Online version:10.1093/emboj/cdf404 |
| Keywords |
Amino Acid Sequence; Amino Acid Substitution; Animals; Calmodulin/chemistry; Calmodulin/physiology; Catecholamines/secretion; Cattle; Chromaffin Cells/drug effects; Chromaffin Cells/secretion; Exocytosis/drug effects; Exocytosis/physiology; Human Growth Hormone/secretion; Humans; Macromolecular Substances; Membrane Proteins/chemistry; Membrane Proteins/genetics; Membrane Proteins/metabolism; Membrane Proteins/pharmacology; Membrane Proteins/physiology; Metalloendopeptidases/pharmacology; Microinjections; Molecular Sequence Data; PC12 Cells/drug effects; PC12 Cells/secretion; Peptide Fragments/chemical synthesis; Peptide Fragments/pharmacology; Phospholipids/physiology; Protein Structure, Tertiary; R-SNARE Proteins; Rats; Recombinant Fusion Proteins/secretion; SNARE Proteins; Sesterterpenes; Surface Plasmon Resonance; Syntaxin 1; Terpenes/pharmacology; Tetanus Toxin/pharmacology; Transfection; Vesicular Transport Proteins |
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