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Mannose 6-phosphate receptor

Cation-dependent mannose 6-phosphate receptor
Symbol M6PR
Entrez 4074
HUGO 6752
OMIM 154540
RefSeq NM_002355
UniProt P20645
Other data
Locus Chr. 12 p13
This article is about the cation-dependent mannose 6-phosphate receptor. For the cation-independent mannose 6-phosphate receptor, see Insulin-like growth factor 2 receptor

In biochemistry and cell biology, the mannose 6-phosphate receptor (also known as the cation-dependent mannose 6-phosphate receptor, or CD-MPR) is one of two transmembrane proteins that bind mannose-6-phosphate (M6P) tags on acid hydrolase precursors in the Golgi apparatus that are destined for transport to the lysosome. Homologues of CD-MPR are found in all eukaryotes.



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 (Ghosh, Dahms & Kornfeld 2003). The extracytoplasmic/lumenal M6P binding-domain consists of 157 amino acid residues. The CD-MPR is approximately 46 kDa in size and it both exists and functions as a dimer.

Cation-independent mannose 6-phosphate receptor

The cell surface receptor for insulin-like growth factor 2 also functions as a cation-independent mannose 6-phosphate receptor (Ghosh, Dahms & Kornfeld 2003). 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 (Ghosh, Dahms & Kornfeld 2003). The MPRs (bound to their cargo) are recognized by the GGA family of clathrin adaptor proteins and accumulate in forming clathrin-coated vesicles (Ghosh & Kornfeld 2004). 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.


Ghosh, Pradipta; Dahms, Nancy H. & Kornfeld, Stuart (2003), " ", Nature Reviews Molecular and Cell Biology 4: 203-121, PMID 12612639

Ghosh, Pradipta & Kornfeld, Stuart (2004), " ", European Journal of Cell Biology 83: 257-262, PMID 15511083

This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Mannose_6-phosphate_receptor". A list of authors is available in Wikipedia.
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