cation-dependent mannose-6-phosphate receptor

The CD-MPR is a type I transmembrane protein (that is, it has a single transmembrane domain with its C-termini on the cytoplasmic side of lipid membranes) with a relatively short cytoplasmic tail.{{cite journal |vauthors=Ghosh P, Dahms NM, Kornfeld S | title = Mannose 6-phosphate receptors: new twists in the tale | journal = Nat. Rev. Mol. Cell Biol. | volume = 4 | issue = 3 | pages = 202–212 | date = March 2003 | pmid = 12612639 | doi = 10.1038/nrm1050 | s2cid = 16991464 }} The extracytoplasmic/lumenal M6P binding-domain consists of 157 amino acid residues. The CD-MPR is approximately {{val|46|ul=kDa}} in size and it both exists and functions as a dimer.

The cell surface receptor for insulin-like growth factor 2 also functions as a cation-independent mannose 6-phosphate receptor. It consists of fifteen repeats homologous to the 157-residue CD-M6PR domain, two of which are responsible for binding to M6P.

Both CD-MPRs and CI-MPRs are lectins that bind their M6P-tagged cargo in the lumen of the Golgi apparatus. The CD-MPR shows greatly enhanced binding to M6P in the presence of divalent cations, such as manganese. The MPRs (bound to their cargo) are recognized by the GGA family of clathrin adaptor proteins and accumulate in forming clathrin-coated vesicles.{{cite journal |vauthors=Ghosh P, Kornfeld S | title = The GGA proteins: key players in protein sorting at the trans-Golgi network | journal = Eur. J. Cell Biol. | volume = 83 | issue = 6 | pages = 257–62 | date = July 2004 | pmid = 15511083 | doi = 10.1078/0171-9335-00374 }} They are trafficked to the early endosome where, in the relatively low pH environment of the endosome, the MPRs release their cargo. The MPRs are recycled back to the Golgi, again by way of interaction with GGAs and vesicles. The cargo proteins are then trafficked to the lysosome via the late endosome independently of the MPRs.

• Mannose 6-phosphate receptor

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• {{MeshName|cation-dependent+mannose-6-phosphate+receptor}}

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