Doc2γ, a third isoform of double C2 protein, lacking calcium-dependent phospholipid binding activity

Mitsunori Fukuda, Katsuhiko Mikoshiba

Research output: Contribution to journalArticlepeer-review

32 Citations (Scopus)

Abstract

The Doc2 (double C2) family consists of two isoforms (Doc2α and Doc2β) characterized by an N-terminal Munc13-1 interacting domain (Mid) and two C2 domains that interact with Ca2+ and phospholipid at the C-terminus. This Ca2+-binding property is thought to be important to the regulation of neurotransmitter release. In this paper, we report a third isoform of mouse Doc2, named Doc2γ. Doc2γ also contains a putative Mid domain and two C2 domains, and it is 45.6 and 43.2% identical to mouse Doc2α and Doc2β, respectively, at the amino acid level. In contrast to the other Doc2 isoforms, the C2 domains of Doc2γ impair Ca2+-dependent phospholipid binding activity. The highest expression of Doc2γ mRNA was found in the heart, but occurs ubiquitously, the same as Doc2β. These findings indicate that Doc2γ may also function as an effector for Munc13-1 and that it may be involved in the regulation of vesicular trafficking. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)626-632
Number of pages7
JournalBiochemical and biophysical research communications
Volume276
Issue number2
DOIs
Publication statusPublished - 2000 Sep 24
Externally publishedYes

Keywords

  • C2 domain
  • Doc2
  • Exocytosis
  • Phospholipid binding
  • Rabphilin
  • Synaptotagmin

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Doc2γ, a third isoform of double C2 protein, lacking calcium-dependent phospholipid binding activity'. Together they form a unique fingerprint.

Cite this