Spring, a novel RING finger protein that regulates synaptic vesicle exocytosis.
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.
Mesh Terms:
Amino Acid Sequence, Animals, Antigens, Surface, Binding, Competitive, Brain, CHO Cells, Calcium, Carrier Proteins, Cricetinae, DNA, Complementary, Exocytosis, Membrane Proteins, Molecular Sequence Data, Nerve Tissue Proteins, PC12 Cells, R-SNARE Proteins, RNA, Messenger, Rats, Sequence Homology, Amino Acid, Synaptic Vesicles, Synaptosomal-Associated Protein 25, Syntaxin 1, Two-Hybrid System Techniques
Amino Acid Sequence, Animals, Antigens, Surface, Binding, Competitive, Brain, CHO Cells, Calcium, Carrier Proteins, Cricetinae, DNA, Complementary, Exocytosis, Membrane Proteins, Molecular Sequence Data, Nerve Tissue Proteins, PC12 Cells, R-SNARE Proteins, RNA, Messenger, Rats, Sequence Homology, Amino Acid, Synaptic Vesicles, Synaptosomal-Associated Protein 25, Syntaxin 1, Two-Hybrid System Techniques
J. Biol. Chem.
Date: Nov. 02, 2001
PubMed ID: 11524423
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