TY - JOUR
T1 - Identification as β-adducin of a protein interacting with Rabphilin-3A in the presence of Ca2+ and phosphatidylserine
AU - Miyazaki, Mutsuo
AU - Shirataki, Hiromichi
AU - Kohno, Hiđeshi
AU - Kaibuchi, Kozo
AU - Tsugita, Akira
AU - Takai, Yoshimi
PY - 1994
Y1 - 1994
N2 - 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 it 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.
AB - 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 it 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.
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U2 - 10.1006/bbrc.1994.2688
DO - 10.1006/bbrc.1994.2688
M3 - Article
C2 - 7999065
AN - SCOPUS:0028170574
SN - 0006-291X
VL - 205
SP - 460
EP - 466
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -