Identification as beta-adducin of a protein interacting with rabphilin-3A in the presence of Ca2+ and phosphatidylserine

Biochem Biophys Res Commun. 1994 Nov 30;205(1):460-6. doi: 10.1006/bbrc.1994.2688.

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
  • 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
  • rabphilin-3A
  • GTP-Binding Proteins
  • rab GTP-Binding Proteins
  • Calcium