SYT7
SYT7 (synaptotagmin 7, also known as IPCA-7, SYT-VII and PCANAP7) is a calcium sensor of the synaptotagmin family that couples Ca2+ binding to the exocytosis of secretory and synaptic vesicles. It also drives lysosomal exocytosis and synaptic facilitation. Browse Assay Genie's current range of SYT7 research reagents below, or read on for the biology behind the target.
SYT7 is a Ca2+ sensor that regulates Ca2+-dependent exocytosis of secretory and synaptic vesicles. Through its C2 domain, Ca2+ induces binding to phospholipid membranes and to assembled SNARE complexes, and both actions contribute to triggering exocytosis. Compared with other synaptotagmins, SYT7 binds Ca2+ with high affinity and slow kinetics. In chromaffin cells it promotes fusion pore opening and expansion, and it also regulates some non-synaptic secretory granules of specialised cells.
At synapses, SYT7 is a key mediator of synaptic facilitation, or short-term synaptic potentiation. This occurs at synapses with a low initial release probability, where Ca2+ influx after spike generation raises the probability of neurotransmitter release. SYT7 probably acts by directly increasing release probability, and it may also contribute by supporting synaptic vesicle replenishment as a Ca2+ sensor that forms a complex with calmodulin. It also regulates Ca2+-dependent insulin and glucagon secretion in beta-cells.
Beyond neurons, SYT7 mediates Ca2+-triggered lysosomal exocytosis, a major component of plasma membrane repair. This delivery of lysosomal membranes to the cell surface contributes to phagocytic uptake by macrophages, to bone remodelling through secretory pathways in osteoclasts and osteoblasts, and to cell invasion by Trypanosoma cruzi. SYT7 is also involved in cholesterol transport from lysosome to peroxisome, promoting membrane contacts probably by binding phosphatidylinositol-4,5-bisphosphate on peroxisomal membranes. The human gene belongs to the synaptotagmin gene group, was formerly named prostate cancer associated protein 7, and its expression has been associated with prostate cancer. Alternatively spliced transcript variants encoding multiple isoforms have been observed.
SYT7 is a key mediator of synaptic facilitation and may support synaptic vesicle replenishment, making it central to short-term potentiation studies.
Ca2+-triggered lysosomal exocytosis via SYT7 is a major component of plasma membrane repair and of macrophage phagocytic uptake.
SYT7 regulates Ca2+-dependent insulin and glucagon secretion in beta-cells, relevant to hormone release research.
SYT7 promotes lysosome–peroxisome membrane contacts and cholesterol transport from lysosome to peroxisome.
SYT7 is a Ca2+ sensor that triggers Ca2+-dependent exocytosis of secretory and synaptic vesicles by binding phospholipids and SNARE complexes. It mediates synaptic facilitation, lysosomal exocytosis for membrane repair, and regulates insulin and glucagon secretion in beta-cells.
SYT7 is also called synaptotagmin VII, SYT-VII, IPCA-7, PCANAP7 and MGC150517. Earlier names include prostate cancer associated protein 7. The gene has alternatively spliced transcript variants that encode multiple isoforms, so check the datasheet of any product for its validated reactivity.
SYT7 has mouse and rat orthologs, both named Syt7, and rodent protein mediates hormone secretion and lysosome exocytosis. In humans, SYT7 expression has been associated with prostate cancer, and the protein is involved in Trypanosoma cruzi cell invasion.
Other synaptotagmin family members that regulate Ca2+-dependent membrane trafficking and vesicle exocytosis.
Gene and protein annotations from HGNC, NCBI Gene and UniProt O43581; product specifications from Assay Genie datasheets.