Synaptotagmin-like protein 1 (SYTL1)

Synaptotagmin-like protein 1 (SYTL1) is a membrane-associated protein that functions primarily as an effector in vesicle trafficking and exocytosis, especially in secretory cells. It contains a Rab-binding domain at the N-terminus and two tandem C2 domains at the C-terminus, facilitating interactions with Rab GTPases such as Rab27A and Rab8 as well as plasma membrane phosphoinositides[1][6][7]. SYTL1 is involved in the docking and fusion of secretory granules with cellular membranes, playing a role in immune responses (cytotoxic granule exocytosis in lymphocytes), secretion regulation in various cell types, and can interact with partners such as neurexins and syntaxins[1][6][7][11]. Its expression and phosphorylation pattern have been linked to specific cancers, where higher expression may serve as a favorable prognostic biomarker[6]. However, SYTL1 is not currently established as a direct therapeutic target and there are no approved drugs known to interact with it as of now. \n\nIf further drug or clinical information becomes available, these entries may require updating.

Other names

Synaptotagmin-like protein 1SYTL1SLP1SB146JFC1FLJ14996Exophilin-7Protein JFC1NADPH oxidase-related C2 domain-containing protein

not established as a drug target; drugs impacting SYTL1 would likely affect vesicular trafficking or exocytosis if developed