Sortilin/SORT1 Protein, Human (Biotinylated, HEK293, His-Avi)

Sortilin (SORT1) protein functions both as a sorting receptor within the Golgi compartment and as a clearance receptor on the cell surface. It plays a crucial role in protein transport from the Golgi apparatus to lysosomes, independent of the mannose-6-phosphate receptor (M6PR). In this process, lysosomal proteins specifically bind to the receptor in the Golgi, forming a receptor-ligand complex that is transported to an acidic prelysosomal compartment. The low pH in this compartment mediates complex dissociation, and the receptor is recycled back to the Golgi via binding to the retromer. Additionally, Sortilin is involved in protein transport from the Golgi to endosomes. It facilitates neuronal apoptosis by mediating the endocytosis of proapoptotic precursor forms of BDNF and NGFB, while also acting as a receptor for neurotensin. In adipocytes, Sortilin is likely required for the formation of specialized storage vesicles containing the glucose transporter SLC2A4 (GLUT4), enhancing responsiveness to insulin. The protein interacts with various partners, including ligands like LRPAP1/RAP, GM2A, and NTS, as well as participating in a complex with NGFR. Sortilin also engages with cytosolic adapter proteins, such as GGA1 and GGA2, and forms interactions with proteins like CLN5, PSAP, GRN, and SMPD1, contributing to its diverse cellular functions.