Synaptotagmin II. A novel differentially distributed form of synaptotagmin

Cellubrevin and synaptobrevins: similar subcellular localization and biochemical properties in PC12 cells.

“…It appears therefore that synaptobrevin 1 and 2 and cellubrevin share a similar function and may be present in different combinations on the same vesicular carriers as was previously shown for other synaptic vesicle-associated proteins (Sudhof et al, 1989;Geppert et al, 1991;Fykse et al, 1993;Bajjalieh et al, 1993). Isoform specific characteristics may contribute to the fine tuning of the function of exocytotic carriers but do not appear to contribute major functional differences.…”

Palmitoylation-dependent association with CD63 targets the Ca2+ sensor synaptotagmin VII to lysosomes

“…Trafficking of the neuronal isoform Syt I to synaptic vesicles (Matthew et al, 1981;Kabayama et al, 1999) was attributed to a dihydrophobic methionine-leucine motif within its extreme C terminus (Blagoveshchenskaya et al, 1999), although posttranslational modifications at the N terminus such as N-glycosylation (Han et al, 2004), O-glycosylation (Fukuda, 2002;Kanno and Fukuda, 2008), and palmitoylation (Heindel et al, 2003;Kang et al, 2004) were also proposed to play a role. The trafficking of Syt II (Geppert et al, 1991) to neurite terminals was also linked to a C-terminal two-residue motif (Krasnov and Enikolopov, 2000), whereas a unique region within the spacer domain of Syt IV was found to be necessary for Golgi targeting in PC-12 cells (Fukuda et al, 2001a). Syt IX, an isoform reported to control the exocytosis of -cell granules (Iezzi et al, 2004) and dense core vesicles in PC-12 cells (Fukuda et al, 2004), is sorted to recycling endosomes in RBL-2H3 and CHO cell lines by a mechanism dependent on PKC-mediated phosphorylation (Haberman et al, 2005).…”

Regulation of Membrane Fusion in Synaptic Excitation-Secretion Coupling: Speed and Accuracy Matter

“…Its C2A and C2B domains complex Ca 2+ ions and interact with phospholipid membranes in a Ca 2+ -dependent manner (Bai and Chapman, 2004;Brose et al, 1992;Perin et al, 1990). Studies in Drosophila and mouse have shown that Synaptotagmin 1 functions as the Ca 2+ sensor in regulated exocytosis, and the highly homologous mammalian Synaptotagmin 2 (Geppert et al, 1991) appears to perform an analogous function (Pang et al, 2006). Genetic deletion of Synaptotagmin 1 in flies and mice severely impairs the fast component of evoked neurotransmitter release that occurs in synchrony with the peak of presynaptic Ca 2+ influx (Broadie et al, 1994;Geppert et al, 1994;Littleton et al, 1993;Loewen et al, 2001;Nishiki and Augustine, 2004;Yoshihara and Littleton, 2002).…”