Abstract
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 beta-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 beta-adducin in the presence of Ca2+ and phosphatidylserine.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Adaptor Proteins, Signal Transducing
-
Amino Acid Sequence
-
Animals
-
Brain / metabolism
-
Calcium / metabolism*
-
Calmodulin-Binding Proteins / metabolism*
-
Cattle
-
GTP-Binding Proteins / chemistry
-
GTP-Binding Proteins / metabolism*
-
Humans
-
Molecular Sequence Data
-
Nerve Tissue Proteins / chemistry
-
Nerve Tissue Proteins / metabolism*
-
Phosphatidylserines / metabolism*
-
Protein Conformation
-
Rabphilin-3A
-
Rats
-
Sequence Homology, Amino Acid
-
Vesicular Transport Proteins
-
rab GTP-Binding Proteins*
Substances
-
Adaptor Proteins, Signal Transducing
-
Calmodulin-Binding Proteins
-
Nerve Tissue Proteins
-
Phosphatidylserines
-
Vesicular Transport Proteins
-
adducin
-
GTP-Binding Proteins
-
rab GTP-Binding Proteins
-
Calcium