Post-Translational Modifications Essay

Post-Translational Modifications Essay

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Post-translational modifications have a profound influence on the structure and function of many proteins. Dystroglycan (DG) is an example of a membrane protein that requires extensive post-translational processing in order to function as an extracellular matrix receptor. It is comprised of two subunits, an extracellular -DG subunit and a transmembrane -DG subunit, which are derived by cleavage of a polypeptide encoded by DAG1 (1). The apparent molecular mass (Mr) of -DG as assessed by SDS-PAGE varies from 120- to 200-kDa, due to developmental and tissue-specific post-translational modification of an ~40-kDa core polypeptide (1, 2). Notably, in both muscle and brain, -DG serves as a receptor for extracellular matrix ligands that contain a laminin-G domain—including laminin (1), agrin (3), perlecan (4), and neurexins (5)—and this interaction depends on an unidentified post-translational modification on -DG. -DG is also known as the cellular receptor for lymphocytic choriomeningitis virus (LCMV), Lassa fever virus (LFV), and clade C New World arenaviruses (6, 7). Although the binding sites for LCMV and LFV on -DG have not yet been identified, they are thought to overlap with the modification that is recognized by laminin (8, 9). Mutations in six known or putative glycosyltransferase genes—POMT1 (10), POMT2 (11), POMGnT1 (12), fukutin (13), FKRP (14), and LARGE (15) —have been identified in patients with congenital muscular dystrophies (CMD) classified as “secondary -dystroglycanopathy”. These disorders cover a spectrum of abnormalities affecting the brain, eye, and skeletal muscle, and show a dramatic gradient of phenotypic severity that ranges from the most devastating in Walker-Warburg syndrome (WWS; OMIM# 236670), to...

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...e in vertebrates. Glycoproteins in the cell wall of yeasts and fungi are known to bear phosphodiester-linked glycans that are generated by a process involving phosphorylation on the C6 position of mannose (28). It is interesting that -DG, which is well conserved as an epithelial cell-surface protein from mammals to lower vertebrates, is likewise modified by this ancient type of cell surface glycosylation. A recent study has shown that the most severe form of CMD—WWS—is a genetically heterogeneous disease. Moreover, only 40% of WWS cases are explained by mutations in known CMD-causative genes (POMT1, POMT2, POMGNT1, FCMD, FKRP and LARGE) (28). It is quite likely that a defect in the phosphorylation of O-linked mannose results in severe CMD, and thus our findings provide a new target to be used for the discovery of mutations in novel genes responsible for WWS.

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