Mammalian O-mannosylation pathway: glycan structures, enzymes, and protein substrates.
The mammalian O-mannosylation pathway for protein post-translational modification is intricately involved in modulating cell-matrix interactions in the musculature and nervous system. Defects in enzymes of this biosynthetic pathway are causative for multiple forms of congenital muscular dystophy. 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. 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. Also, we attempt to highlight key outstanding questions raised by this abundance of new information.
Complex Carbohydrate Research Center, Department of Biochemistry and Molecular Biology, The University of Georgia , Athens, Georgia 30602, United States.
Jeremy L
JL
Praissman
Lance
L
Wells
D000818:Animals; D002236:Carbohydrate Conformation; D006031:Glycosylation; D006801:Humans; D008358:Mannose / Q000737:chemistry / Q000378:metabolism*; D008364:Mannosyltransferases / Q000737:chemistry / Q000378:metabolism*; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism*; D011499:Protein Processing, Post-Translational / Q000502:physiology*
D011134:Polysaccharides; D008364:Mannosyltransferases; D008358:Mannose