Printer friendly
"AcronymAttic.com

What does M6PRs stand for?

M6PRs stands for CD)-mannose 6-phosphate receptors

This definition appears rarely

Samples in periodicals archive:

45) will remove the GlcNAc residue exposing the mannose 6-phosphate tag, allowing the lysosomal enzymes to bind to the CI-MPR and the CD-MPR. The MPR-lysosomal enzyme complex is translocated to a pre-lysosomal compartment, known as an endosome, in a clathrin-coated vesicle. [11][12] This targeting away from the secretory pathway is achieved by the presence of a specific sorting signal, an acidic cluster/dileucine motif, in the cytoplasmic tails of the MPRs. [13] Both MPRs bind their ligands most effectively at pH 6 – 7; thus enabling the receptors to bind to the lysosomal enzymes in the trans-Golgi and release them in the acidified environment of the endosome. Once the enzyme has dissociated from the mannose 6-phosphate receptor.
The cell surface receptor for insulin-like growth factor 2 also functions as a cation-independent mannose 6-phosphate receptor. [3] It consists of fifteen repeats homologous to the 157-residue CD-M6PR domain, two of which are responsible for binding to M6P.
We discuss what is known about the roles of these Rab proteins and their interacting partners on the regulation of traffic of important receptor proteins such as the epidermal growth factor receptor (EGFR) and the mannose 6-phosphate receptor.
Transport of lysosomal enzymes is mediated by two mannose 6-phosphate receptors: a cation dependent (CD-MPR) and a cation independent receptor (CI-MPR). In the present study the effect of MPR-deficiency on the lysosomal system of neonatal mouse hepatocytes was studied by ultrastructural morphometric analyses.
a | The non-ligand-bound form of the cation-dependent mannose 6-phosphate (M6P) receptor (CD-MPR) shows several significant conformational changes as compared to b | the ligand-bound form. In the ligand-free form, loop D — which encompasses residues E134–C141 — bends into the unoccupied M6P-binding cleft. This reorientation of loop D results in the formation of an intricate network of hydrogen bonds that seems to maintain the integrity of the binding site and keep the side chains of three of the four residues that are essential for carbohydrate recognition in position to bind the ligand.