Spring, a novel RING finger protein that regulates synaptic vesicle exocytosis.

Authors: Li, Y  Chin, LS  Weigel, C  Li, L 
Citation: Li Y, etal., J Biol Chem 2001 Nov 2;276(44):40824-33.
Pubmed: (View Article at PubMed) PMID:11524423
DOI: Full-text: DOI:10.1074/jbc.M106141200

The synaptosome-associated protein of 25 kDa (SNAP-25) interacts with syntaxin 1 and vesicle-associated membrane protein 2 (VAMP2) to form a ternary soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor (SNARE) complex that is essential for synaptic vesicle exocytosis. We report a novel RING finger protein, Spring, that specifically interacts with SNAP-25. Spring is exclusively expressed in brain and is concentrated at synapses. The association of Spring with SNAP-25 abolishes the ability of SNAP-25 to interact with syntaxin 1 and VAMP2 and prevents the assembly of the SNARE complex. Overexpression of Spring or its SNAP-25-interacting domain reduces Ca(2+)-dependent exocytosis from PC12 cells. These results indicate that Spring may act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP-25 for the SNARE complex formation.

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CRRD Object Information
CRRD ID: 631246
Created: 2003-08-04
Species: All species
Last Modified: 2003-08-04
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.