Rabphilin 3A and Doc2α are synaptic vesicle-associated proteins, and are thought to function as Ca2+ sensors in neurotransmitter release. If either rabphilin 3A or Doc2α plays a role in membrane trafficking, like the synaptotagmins, then non-neural forms should be present. Here we describe the isolation of a mouse cDNA which encodes a novel Doc2 homologue (Doc2β) that is present in all tissues. The encoded protein, which is highly homologous to human Doc2α (70% identity), is composed of 412 amino acids with a calculated relative molecular mass (M(r)) of 45,837. The sequence identity is especially high in two C2 domains (74% in C2A and 84% in C2B). Northern and Western blot analyses have shown that Doc2β is expressed in all cell lines and tissues tested. Ca2+-dependent phospholipid binding assaying of recombinant fusion proteins revealed that the single C2A domain, but not the C2B domain, of Doc2β binds phosphatidycholine and phosphatidylserine (2.5:1, w/w) liposomes. The binding is Ca2+-dependent, with an EC50 value of approximately 1 μM and a Hill coefficient of approximately 3, which are comparable to those of synaptotagmins, rabphilin 3A and Doc2α. Our results suggest that Doc2β is involved in constitutive membrane trafficking.
|Number of pages||6|
|Journal||Journal of Biochemistry|
|Publication status||Published - 1996 Jan 1|
- C2 domain
- Rabphilin 3A
ASJC Scopus subject areas
- Molecular Biology