Mannose 6-phosphate receptor (M6PR) is encoded in humans by the M6PR gene. In the field of biochemistry and cell biology, it is also known as the cation-dependent mannose-6-phosphate receptor (CD-MPR). M6PR is a type I transmembrane protein with a single transmembrane domain and a C-terminus located on the cytoplasmic side of the lipid membrane. M6PR is approximately 46 kDa in size and has a relatively short cytoplasmic tail with a cytoplasmic M6P binding domain consisting of 157 amino acid residues, which is involved in dimerization.
|Basic Information of M6PR|
|Protein Name||Cation-dependent mannose-6-phosphate receptor|
|Aliases||CD-MPR, MPR46, SMPR, CD-mannose-6-phosphate receptor, cation dependent|
|Organism||Homo sapiens (Human)|
The primary function of M6PR is the sorter and deliverer of lysosomal enzymes. The lysosomal enzymes are sorted and delivered by receptor-mediated transport by binding to the extracellular domain of M6PR. Lysosomal enzymes are transported to lysosomes via two M6PR-dependent pathways. One pathway is that the lysosomal enzyme marker M6P in the Golgi complex is combined with M6PR and then transported into the Golgi apparatus. The other pathway is the binding of M6P-containing lysosomes in the extracellular matrix to M6PR on the cell membrane to transport lysosomal enzymes. In both pathways, a receptor-ligand complex is formed by binding of a lysosomal enzyme to M6PR and then transported to a lysosome. Besides, in a low pH environment, the receptor and ligand are separated and the M6PR is recycled back to the Golgi complex or plasma membrane.
Fig.1 The structure of M6PR.
The authors observed that M6PR and Sortilin bound to immobilized CS and concluded that CI-MPR was involved in lysozyme and granule-targeted serum glycine and basic proteins, such as lysozymes associated with proteoglycans in hematopoietic cells.
The article found that intracellular MPRci appeared to transfer the newly enveloped VZV to late endosomes, suggesting that the plasma membrane MPRci is required for cell-free VZV entry.
The study showed that the expression of M6P / IGF2R mRNA in HCC tissues of HBV-positive patients was lower than that of non-tumor tissues, suggesting that M6P / IGF2R may participate in the level of HBV-related hepatocarcinogenesis through the regulation of its expression.
The authors isolated a cDNA clone encoding the entire sequence of the bovine 46kd cation-dependent mannose 6-phosphate (CD Man-6-P) receptor and found that it may contain 279 amino acid sequences, a peptide containing a signal peptide sequence and a transmembrane domain.
The authors isolated a complementary DNA clone of human cation-dependent mannose 6-phosphate-specific receptor from a human placental library of λgt11 and performed related biological information analysis.
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