Synaptotagmin-10 (SYT10) belongs to the synaptotagmin family, which is a group of membrane-trafficking proteins that contain two C-terminal C2 domains. Most of the synaptotagmins have a unique N-terminal domain that is involved in membrane anchoring or specific ligand binding. SYT10 localises to olfactory bulb and controls the Ca(2+)-dependent exocytosis that is spatially and temporally distinct from Ca(2+)-dependent synaptic vesicle exocytosis controlled by SYT1 [].
ZDHHC17 (also known as HIP14, huntingtin-interacting protein 14) is a palmitoyl acyltransferase (PAT) specific for a subset of neuronal proteins, including SNAP25, DLG4/PSD95, GAD2, SYT1 and HD. It may play a role in the pathogenesis of Huntington disease []. It also mediates Mg2+ transport and may play a role in cellular magnesium homeostasis [].
Synaptotagmin-12 (Syt12) belongs to the synaptotagmin family, which is a group of membrane-trafficking proteins that contain two C-terminal C2 domains (known as C2A and C2B domains). Most of the synaptotagmins have a unique N-terminal domain that is involved in membrane anchoring or specific ligand binding. Mammals contain 16 synaptotagmins; eight of these bind Ca2+ via their C2-domains (Syt1-Syt3, Syt5-7, Syt9, and Syt10), whereas the other eight, including Syt12, do not [].Syt12 colocalises with and binds Syt1 on synaptic vesicles, but regulates spontaneous release independently from Syt1. Syt12 is phosphorylated by cAMP-dependent protein kinase A (PKA) at a single site, and mutation of this site blocks the effect of Syt12 on spontaneous release []. Syt12 is not essential for basal synaptic transmission, but is required for cAMP-dependent mossy fibre long-term potentiation (LTP), a presynaptic form of long-term plasticity that is induced by PKA activation [].
