A complex of rab3A, SNAP-25, VAMP/synaptobrevin-2 and syntaxins in brain presynaptic terminals

Two monoclonal antibodies (SPM-1 and SPM-2) immunoprecipitate brain N-type calcium channels. On immunoaffinity chromatography of digitonin extracts of bovine brain membranes on SPM-1- and SPM-2-Sepharose, proteins of 36 (syntaxins A and B), 28 and 19 kDa are specifically retained by both columns. He...

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Veröffentlicht in:	FEBS letters 1993-09, Vol.330 (2), p.236-240
Hauptverfasser:	Horikawa, Hiroshi P.M., Saisu, Hideo, Ishizuka, Toru, Sekine, Yoko, Tsugita, Akira, Odani, Shoji, Abe, Teruo
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Antigens, Surface - analysis Antigens, Surface - chemistry Biological and medical sciences Brain Chemistry Cattle Cell physiology Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology GTP-Binding Proteins - analysis GTP-Binding Proteins - chemistry Membrane Proteins - analysis Membrane Proteins - chemistry Molecular and cellular biology Molecular Sequence Data Nerve Tissue Proteins - analysis Nerve Tissue Proteins - chemistry Neurotransmission Neurotransmitter release R-SNARE Proteins rab3 GTP-Binding Proteins Rab3A/smg25A SNAP-25 Synapses - chemistry Synaptosomal-Associated Protein 25 Syntaxin Syntaxin 1 VAMP/synaptobrevin-2
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Zusammenfassung:	Two monoclonal antibodies (SPM-1 and SPM-2) immunoprecipitate brain N-type calcium channels. On immunoaffinity chromatography of digitonin extracts of bovine brain membranes on SPM-1- and SPM-2-Sepharose, proteins of 36 (syntaxins A and B), 28 and 19 kDa are specifically retained by both columns. Here we show that the 19 and 28 kDa bands contain VAMP/synaptobrevin-2, and rab3A/smg25A and SNAP-25, respectively. Since SPM-1 and SPM-2 recognize only syntaxins and the 28 kDa band (rab3A/smg25A and SNAP-25), respectively, the results indicate that all these proteins form a complex. Our results suggest tight linkage between the components involved in neurotransmitter release.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(93)80281-X