Identification as β-Adducin of a Protein Interacting with Rabphilin-3A in the Presence of Ca2+ and Phosphatidylserine

Rabphilin-3A is a putative target protein for Rab3A small GTP-binding protein implicated in neurotransmitter release. We have previously identified a Rabphilin-3A-interacting protein with a Mr of about 115 kDa in bovine brain. We have attempted here to purify this protein and to determine its primar...

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Veröffentlicht in:Biochemical and biophysical research communications 1994-11, Vol.205 (1), p.460-466
Hauptverfasser: Miyazaki, M., Shirataki, H., Kohno, H., Kaibuchi, K., Tsugita, A., Takai, Y.
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Sprache:eng
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Zusammenfassung:Rabphilin-3A is a putative target protein for Rab3A small GTP-binding protein implicated in neurotransmitter release. We have previously identified a Rabphilin-3A-interacting protein with a Mr of about 115 kDa in bovine brain. We have attempted here to purify this protein and to determine its primary structure. Amino acid sequence analysis has revealed that this protein is a bovine counterpart of human β-adducin which is known to be a good substrate for protein kinase C. The Rabphilin-3A-interacting protein also binds to protein kinase C in the presence of Ca2+ and phosphatidylserine. These results indicate that Rabphilin-3A binds to β-adducin in the presence of Ca2+ and phosphatidylserine.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1994.2688