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

Mutsuo Miyazaki, Hiromichi Shirataki, Hiđeshi Kohno, Kozo Kaibuchi, Akira Tsugita, Yoshimi Takai

Research output: Contribution to journalArticlepeer-review

37 Citations (Scopus)

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 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.

Original languageEnglish
Pages (from-to)460-466
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume205
Issue number1
DOIs
Publication statusPublished - 1994
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Identification as β-adducin of a protein interacting with Rabphilin-3A in the presence of Ca2+ and phosphatidylserine'. Together they form a unique fingerprint.

Cite this