| First Author | Fukuda M | Year | 2001 |
| Journal | Biochem Biophys Res Commun | Volume | 281 |
| Issue | 5 | Pages | 1226-33 |
| PubMed ID | 11243866 | Mgi Jnum | J:68115 |
| Mgi Id | MGI:1932155 | Doi | 10.1006/bbrc.2001.4512 |
| Citation | Fukuda M, et al. (2001) Synaptotagmin-like protein 1-3: a novel family of c-terminal-type tandem c2 proteins. Biochem Biophys Res Commun 281(5):1226-33 |
| abstractText | Synaptotagmins (Syt), rabphilin-3A, and Doc2 belong to a family of carboxyl terminal type (C-type) tandem C2 proteins and are thought to be involved in vesicular trafficking. We have cloned and characterized a novel family of C-type tandem C2 proteins, designated Slp1-3 (synaptotagmin-like protein 1-3). The Slp1-3 C2 domains show high homology to granuphilin-a C2 domains, but the amino-terminal domain of Slp1-3 does not contain any known protein motifs or a transmembrane domain. A subcellular fractionation study indicated that Slp1-3 proteins are peripheral membrane proteins. Phospholipid binding experiments indicated that Slp3 is a Ca(2+)-dependent isoform, but Slp1 and Slp2 are Ca(2+)-independent isoforms, because only the Slp3 C2A domain showed Ca(2+)-dependent phospholipid binding activity. The C-terminus of Slp1-3 also bound neurexin Ialpha in vitro, in the same manner as Syt family proteins, which may be important for the membrane association of Slp1-3. In addition, Slp family proteins are differentially distributed in different mouse tissues and at different developmental stages. Copyright 2001 Academic Press. |
