Glycosylation constitutes one of the most important of all the post-translational modifications and may have numerous effects on the function, structure, physical properties and targeting of particular proteins. Eukaryotic glycan structures are progressively elaborated in the secretory pathway. Following the addition of a core N-linked carbohydrate in the endoplasmic reticulum, glycoproteins move to the Golgi complex where the elongation of O-linked sugar chains and processing of complex N-linked oligosaccharide structures take place. In order to better define how such post-translational modifications occur, we have been studying the yeast KTR and MNN1 mannosyltransferase gene families. The KTR family contains nine members: KRE2, YUR1, KTR1, KTR2, KTR3, KTR4, KTR5, KTR6 and KTR7. The MNN1 family contains six members: MNN1, TTP1, YGL257c, YNR059w, YIL014w and YJL86w. In this review, we address protein structure, sequence similarities and enzymatic activity in the context of each gene family. In addition, a description of the known function of many family members in O- and N-linked glycosylation is included. Finally, the genetic interactions and functional redundancies within a gene family are also discussed.
|Evidence ID||Analyze ID||Interactor||Interactor Systematic Name||Interactor||Interactor Systematic Name||Type||Assay||Annotation||Action||Modification||Phenotype||Source||Reference||Note|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Gene Ontology Term||Gene Ontology Term ID||Qualifier||Aspect||Method||Evidence||Source||Assigned On||Reference||Annotation Extension|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Phenotype||Experiment Type||Experiment Type Category||Mutant Information||Strain Background||Chemical||Details||Reference|
|Evidence ID||Analyze ID||Regulator||Regulator Systematic Name||Target||Target Systematic Name||Experiment||Conditions||Strain||Source||Reference|