MANNOSE 6-PHOSPHATE RECEPTORS: NEW TWISTS IN THE TALE Nature Reviews Molecular Cell Biology 4, 202 -213 (2003) | |
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The two mannose 6-phosphate (M6P) receptors were identified because of their ability to bind M6P-containing soluble acid hydrolases in the Golgi and transport them to the endosomal–lysosomal system. During the past decade, we have started to understand the structural features of these receptors that allow them to do this job, and how the receptors themselves are sorted as they pass through various membrane-bound compartments. But trafficking of acid hydrolases is only part of the story. Evidence is emerging that one of the receptors can regulate cell growth and motility, and that it functions as a tumour suppressor  (Рис.1.) | The MPRs are type-I transmembrane glycoproteins.  (Рис.2.) | The crystal structure of the extracytoplasmic region of the bovine CD-MPR.  (Рис.3.) | Comparison of the CI-MPR domain 11 and CD-MPR structures.  (Рис.4.) | A schematic representation of the subcellular localization and trafficking itinerary of the MPRs.  (Рис.5.) | Sorting signals on MPR tails.  (Рис.6.) | The structure of the GGA3 VHS domain bound to its ligand.  (Рис.7.) | Architecture of the trans-Golgi network and its relevance to MPR trafficking.
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