Mannosyl- and Xylosyl-Containing Glycans Promote Tomato (Lycopersicon esculentum Mill.) Fruit Ripening Also, we attempt to highlight key outstanding questions raised by this abundance of new information. In this review, we will highlight recent progress focusing on the dramatic expansion of the set of genes known to be involved in O-mannosylation and disease processes, the concurrent acceleration of the rate of O-mannosylation pathway protein functional assignments, the tremendous increase in the number of proteins now known to be modified by O-mannosylation, and the recent progress in protein O-mannose glycan quantification and site assignment. The application of advanced genetic and biochemical technologies has resulted in remarkable progress in this field over the past few years, culminating with the publication of three landmark papers in 2013 alone. Defects in enzymes of this biosynthetic pathway are causative for multiple forms of congenital muscular dystophy. The mammalian O-mannosylation pathway for protein post-translational modification is intricately involved in modulating cell–matrix interactions in the musculature and nervous system. Mammalian O-Mannosylation Pathway: Glycan Structures, Enzymes, and Protein Substrates This article is part of a Special Issue entitled Neuro-glycoscience, edited by Kenji Kadomatsu and Hiroshi Kitagawa. These studies will further contribute to the understanding of the pathomechanism of α-dystroglycanopathy and the development of glycotherapeutics. These findings have opened up a new field in glycoscience. O-mannosyl glycan has a novel, unique structure that is important for the maintenance of brain and muscle functions. Recent studies have revealed that the entire structure of core M3 glycan, including ribitol-5-phosphate, is a novel structure in mammals its unique biosynthetic pathway has been elucidated by the identification of new causative genes for α-dystroglycanopathies and their functions. This review presents recent findings about the structure, biosynthesis, and pathology of O-mannosyl glycans. Although many dystroglycanopathy genes are involved in core M3 processing, the structure and biosynthesis of core M3 glycan remains only partially understood. Recent studies have revealed various O-mannosyl glycan structures, which can be classified as core M1, core M2, and core M3 glycans. Defects in O-mannosyl glycan on α-DG are the primary cause of a group of congenital muscular dystrophies, which are collectively termed α-dystroglycanopathy. O-mannosyl glycans have been found in a limited number of glycoproteins of the brain, nerves, and skeletal muscles, particularly in α-dystroglycan (α-DG). Glycosylation with ribitol-phosphate in mammals: New insights into the O-mannosyl glycan. In addition, we identified neurexin 3, a cell adhesion protein involved in synaptic plasticity, and inter-alpha-trypsin inhibitor 5, a protease inhibitor important in stabilizing the extracellular matrix, as new O-mannosylated glycoproteins. Among the candidates identified are members of the cadherin and plexin superfamilies and the perineural net protein neurocan. Using a mass spectrometry-based approach, we further identified glycoproteins from the murine brain that bear single O-mannose residues. Using this tool, we observed that mono- O-mannosyl glycans occur ubiquitously throughout the murine brain but are especially enriched at inhibitory GABAergic neurons and at the perineural nets. Detailed characterization of clone RKU-1-3-5 revealed that this monoclonal antibody recognizes O-linked mannose also in different peptide and protein contexts. In the present study, rabbit monoclonal antibodies directed against the O-mannosylated peptide YAT(Î☑-Man)AV were generated. Although various O-mannosylated proteins have been identified in the recent years, the distribution of O-mannosyl glycans in the mammalian brain and target proteins are still not well defined. In humans, deficient O-mannosylation results in severe congenital muscular dystrophies often associated with impaired brain and eye development. Protein O-mannosylation is a post-translational modification essential for correct development of mammals. Yu, Jin Liu, Yan Lommel, Mark Möhrlen, Frank Hu, Huaiyu Feizi, Ten Westerlind, Ulrika Ruppert, Thomas Strahl, Sabine Protein O-Mannosylation in the Murine Brain: Occurrence of Mono- O-Mannosyl Glycans and Identification of New Substratesīartels, Markus F.
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