Recombinant Bovine Cation-independent mannose-6-phosphate receptor (IGF2R), partial

Function

Mediates the transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelysosomal compartment where the low pH mediates the dissociation of the complex. The receptor is then recycled back to the Golgi for another round of trafficking through its binding to the retromer. This receptor also binds IGF2. Acts as a positive regulator of T-cell coactivation by binding DPP4

Subcellular Location

Golgi apparatus membrane (Single-pass type I membrane protein); Endosome membrane (Single-pass type I membrane protein)

Subunit

Binds HA-I and HA-II plasma membrane adapters (PubMed:2545438). Interacts with DPP4; the interaction is direct. Binds GGA1, GGA2 and GGA3 (By similarity). Interacts with the heterotrimeric retromer cargo-selective complex (CSC), formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35; which is involved in retrograde trafficking of the receptor from endosomes to the Golgi apparatus (By similarity). Interacts with SNX32; the interaction is involved in intracellular trafficking of the receptor (By similarity)

• Lobel P. et al. Cloning and sequence analysis of the cation-independent mannose 6-phosphate receptor. — J. Biol. Chem. (1988)
• Killian J.K. et al. PubMed: CI-IKI5KS6OHM8K (JAN-)
• Lobel P. et al. Cloning of the bovine 215-kDa cation-independent mannose 6-phosphate receptor. — Proc. Natl. Acad. Sci. U.S.A. (1987)
• Glickman J.N. et al. Specificity of binding of clathrin adapters to signals on the mannose-6-phosphate/insulin-like growth factor II receptor. — EMBO J. (1989)
• Olson L.J. et al. Structure of uPAR, plasminogen, and sugar-binding sites of the 300 kDa mannose 6-phosphate receptor. — EMBO J. (2004)
• Olson L.J. et al. Structural basis for recognition of phosphodiester-containing lysosomal enzymes by the cation-independent mannose 6-phosphate receptor. — Proc. Natl. Acad. Sci. U.S.A. (2010)