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Publication : Synaptotagmin-like protein 5: a novel Rab27A effector with C-terminal tandem C2 domains.

First Author  Kuroda TS Year  2002
Journal  Biochem Biophys Res Commun Volume  293
Issue  3 Pages  899-906
PubMed ID  12051743 Mgi Jnum  J:169802
Mgi Id  MGI:4942255 Doi  10.1016/S0006-291X(02)00320-0
Citation  Kuroda TS, et al. (2002) Synaptotagmin-like protein 5: a novel Rab27A effector with C-terminal tandem C2 domains. Biochem Biophys Res Commun 293(3):899-906
abstractText  Synaptotagmin-like proteins 1-4 (Slp1-4) are new members of the carboxyl-terminal-type (C-type) tandem C2 proteins and are classified as a subfamily distinct from the synaptotagmin and the Doc2 families, because the Slp family contains a unique homology domain at the amino terminus, referred to as the Slp homology domain (SHD). We previously showed that the SHD functions as a binding site for Rab27A, which is associated with human hemophagocytic syndrome (Griscelli syndrome) [J. Biol. Chem. 277 (2002) 9212; J. Biol. Chem. 277 (2002) 12432]. In the present study, we identified a novel member of the Slp family, Slp5. The same as other Slp family members, the SHD of Slp5 preferentially interacted with the GTP-bound form of Rab27A and marginally with Rab3A and Rab6A, both in vitro and in intact cells, but not with other Rabs tested (Rab1, Rab2, Rab4A, Rab5A, Rab7, Rab8, Rab9, Rab10, Rab11A, Rab17, Rab18, Rab20, Rab22, Rab23, Rab25, Rab28, and Rab37). However, unlike other members of the Slp family, expression of Slp5 mRNA was highly restricted to human placenta and liver. Expression of Slp5 protein and in vivo association of Slp5 with Rab27A in the mouse liver were further confirmed by immunoprecipitation. The results suggest that Slp5 might be involved in Rab27A-dependent membrane trafficking in specific tissues.
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