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

First Author  Li Y Year  2001
Journal  J Biol Chem Volume  276
Issue  44 Pages  40824-33
PubMed ID  11524423 Mgi Jnum  J:72535
Mgi Id  MGI:2153221 Doi  10.1074/jbc.M106141200
Citation  Li Y, et al. (2001) Spring, a Novel RING Finger Protein That Regulates Synaptic Vesicle Exocytosis. J Biol Chem 276(44):40824-33
abstractText  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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