A novel alternatively spliced variant of synaptotagmin VI lacking a transmembrane domain. Implications for distinct functions of the two isoforms.
Synaptotagmins are a family of membrane proteins that are characterized by a single transmembrane region and tandem C2 domains and that are likely to regulate constitutive and/or regulated vesicle traffic. We have shown that a subclass of synaptotagmins (III, V, VI, and X) forms homo- and heterodimers through an evolutionarily conserved cysteine motif at their N termini (Fukuda, M., Kanno, E., and Mikoshiba, K. (1999) J. Biol. Chem. 274, 31421-31427). In this study, we identified a novel alternatively spliced variant of synaptotagmin (Syt) VI that lacks the N-terminal 85 amino acids including the transmembrane region (thus designated as Syt VIDeltaTM). Because it lacks the cysteine motif responsible for self-dimerization, Syt VIDeltaTM could not associate with Syt VI even in the presence of Ca(2+). Despite lacking the transmembrane region, Syt VIDeltaTM can associate with the plasma membrane through the C-terminal 29 amino acids. In adult mouse brain, two closely comigrating bands at M(r) approximately 50,000, which closely corresponded to the molecular weight of recombinant Syt VIDeltaTM, were detected by anti-Syt VI antibody. These immunoreactive bands were found in both soluble and membrane fractions of mouse brain, indicating that they are membrane-associated proteins (Syt VIDeltaTM), but not transmembrane proteins (Syt VI). Expression of Syt VI and Syt VIDeltaTM in PC12 or COS-7 cells indicated that the two molecules have a distinct subcellular distribution: Syt VIDeltaTM is present in the cytosol or is associated with the plasma membrane or internal membrane structures, whereas Syt VI is localized to the endoplasmic reticulum and/or Golgi-like perinuclear compartment. These results suggest that Syt VI and Syt VIDeltaTM may play distinct roles in vesicular trafficking.[1]References
- A novel alternatively spliced variant of synaptotagmin VI lacking a transmembrane domain. Implications for distinct functions of the two isoforms. Fukuda, M., Mikoshiba, K. J. Biol. Chem. (1999) [Pubmed]
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