SYT7 (synaptotagmin 7) is a calcium sensor protein that mediates Ca²⁺-dependent exocytosis through its C2 domain, which binds both calcium ions and phospholipids 1. The protein exhibits high-affinity calcium binding with slow kinetics compared to other synaptotagmins and plays crucial roles in multiple cellular processes. SYT7 is essential for synaptic function, mediating synaptic facilitation and neurotransmitter release by directly increasing release probability and regulating synaptic vesicle replenishment 1. The protein also controls lysosomal exocytosis, contributing to plasma membrane repair and phagocytic processes. In pathological contexts, SYT7 dysfunction is linked to neurodegeneration through TDP-43-mediated cryptic splicing, where nuclear TDP-43 depletion leads to aberrant SYT7 splicing and subsequent neuronal dysfunction in diseases like ALS and frontotemporal dementia 12. Clinically, SYT7 is significantly upregulated in various cancers including non-small cell lung cancer, thyroid cancer, and glioblastoma, where high expression correlates with poor prognosis, enhanced tumor proliferation, migration, and metastasis 3456. In cancer contexts, SYT7 promotes exosome secretion and angiogenesis, making it a potential therapeutic target 6.