Clavesin-2 (CLVS2)

Clavesin-2 (CLVS2) is a neuron-specific, membrane-associated protein of the Sec14/CRAL-TRIO family that plays an important role in regulating the morphology of late endosomes and lysosomes in neurons[1][3][7]. It is enriched on clathrin-coated vesicles, where it interacts with clathrin heavy chain and adaptor protein-1 (AP-1), and is involved in the endosomal transport pathway. CLVS2 binds specifically to phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2), a phosphoinositide found in late endosomes and lysosomes, and its deficiency leads to abnormalities in lysosomal compartments, particularly in neuronal cells[1]. CLVS2 is mainly expressed in the central nervous system and is considered essential for maintaining proper endosomal and lysosomal structures in neurons. There is no evidence that CLVS2 is currently a direct therapeutic drug target; there are no known drugs or mechanisms of action or safety concerns linked to it in a clinical context[3][7]. Notes: - CLVS2 is not a receptor, enzyme, transporter, or transcription factor; it is a neuron-specific vesicle-associated lipid-binding protein involved mainly in intracellular trafficking and organelle morphology[1][3][7]. - Aliases are collected from multiple authoritative genomic resources and literature[2][3][5]. - While there are indirect disease associations (such as reference to Fanconi Anemia via pathway analysis), CLVS2 is not directly established as a therapeutic target or disease biomarker[3]. - There are no drugs, mechanisms of action, biomarkers, or safety concerns recorded or recognized for CLVS2 in therapeutic development databases as of the provided information.

Other names

Clavesin-2CLVS2C6orf212C6orf213RLBP1L2bA160A10.4A330019N05RikLOC102724729Retinaldehyde-binding protein 1-like 2clathrin vesicle-associated Sec14 protein 2