... of glycosylation (CDGs), which arise from defects in glycosylation and often manifest as multisystemic phenotypes ( Freeze and Ng, 2011 ; Péanne et al., 2018 ; Reily et al., 2019 ). These have been covered elsewhere, and here, we only highlight certain examples of CDGs that result in a major ECM defect...

...Marcel van Lith; Marie Anne Pringle; Bethany Fleming; Giorgia Gaeta; Jisu Im; Reid Gilmore; Neil J. Bulleid ABSTRACT N-linked glycosylation of proteins entering the secretory pathway is an essential modification required for protein stability and function. Previously, it has been shown...

...Meghana Bhimreddy; Emma Rushton; Danielle L. Kopke; Kendal Broadie ABSTRACT The synaptic cleft manifests enriched glycosylation, with structured glycans coordinating signaling between presynaptic and postsynaptic cells. Glycosylated signaling ligands orchestrating communication are tightly...

... and intrinsic factors. Mucin-type O -glycosylation has been suggested to be a potential factor in the control of ESC pluripotency, and is characterized by the addition of N -acetylgalactosamine (GalNAc) to serine or threonine residues of membrane-anchored proteins and secreted proteins. To date...

... or to parental cells. Further, treatment of cells expressing membranous NIS with specific glycosylation inhibitors highlighted the importance of inherent glycosylation processing and an 84 gene signature glycosylation RT-Profiler array revealed that clones expressing NIS in their membrane cluster separately...

... to loss of adhesion. Adhesion-dependent Arf1 activation regulates its binding to the microtubule minus-end motor protein dynein to control Golgi reorganization, which is blocked by ciliobrevin. Adhesion-dependent Golgi organization controls its function, regulating cell surface glycosylation due to loss...

... migration, autophagy and signalling. Endocytosis Galectin Glycosylation Galectins were discovered based on their galactoside binding activity, in a quest to find proteins that decode complex cell-surface glycans. They were defined as a protein family based on conserved β-galactoside-binding...

...Nicola L. Stevenson; Dylan J. M. Bergen; Roderick E. H. Skinner; Erika Kague; Elizabeth Martin-Silverstone; Kate A. Robson Brown; Chrissy L. Hammond; David J. Stephens ABSTRACT The Golgi is the cellular hub for complex glycosylation, controlling accurate processing of complex proteoglycans...

...Anna Frappaolo; Stefano Sechi; Tadahiro Kumagai; Sarah Robinson; Roberta Fraschini; Angela Karimpour-Ghahnavieh; Giorgio Belloni; Roberto Piergentili; Katherine H. Tiemeyer; Michael Tiemeyer; Maria Grazia Giansanti ABSTRACT Congenital disorders of glycosylation (CDG) comprise a family of human...

... involved in N-linked glycosylation, regulators of ER-Golgi trafficking and proteins involved in immunity. The results of this screening approach led us to address the controversial role of N-linked glycosylation in the transport of Gal-3 to the cell surface. We find that N-linked glycoprotein maturation...

... complexes that crosslink glycosylated ligands to form a dynamic lattice. The galectin lattice regulates the diffusion, compartmentalization and endocytosis of plasma membrane glycoproteins and glycolipids. The galectin lattice also regulates the selection, activation and arrest of T cells, receptor kinase...

... transport system and stable isotope labeling by amino acids in cell culture (SILAC)-based quantitative proteomics.   Mol. Cell. Proteomics   12 , 145 – 157 . 10.1074/mcp.M112.019414 Komekado   H. , Yamamoto   H. , Chiba   T. , Kikuchi   A. ( 2007 ). Glycosylation and palmitoylation...

...Andrew G. McDonald; Jerrard M. Hayes; Tania Bezak; Sonia A. Głuchowska; Eoin F. J. Cosgrave; Weston B. Struwe; Corné J. M. Stroop; Han Kok; Teun van de Laar; Pauline M. Rudd; Keith F. Tipton; Gavin P. Davey ABSTRACT Protein N-glycosylation is a common post-translational modification that produces...

.... Although Wntless (Wls) has been shown to interact with Wnts and support their secretion, the role of Wls in the sorting of Wnts to the final destination in polarized epithelial cells have not been clarified. Glycosylation was shown to be important for the sorting of some transmembrane and secreted proteins...

...Matthew D. Langer; Huabei Guo; Nitesh Shashikanth; J. Michael Pierce; Deborah E. Leckband We present direct evidence that the N-glycosylation state of neural cadherin impacts the intrinsic kinetics of cadherin-mediated intercellular binding. Micropipette manipulation measurements quantified...

... of neuronally expressed IFs and their protein–protein interactions, as well as IF glycosylation, which not only has a role in stress and ageing, but might also regulate IFs during development. Although many of these recent findings are still preliminary, they nevertheless open new doors to explore...

...Catherine L. Jackson The Golgi complex is the central sorting and processing station of the secretory pathway, ensuring that cargo proteins, which are synthesized in the endoplasmic reticulum, are properly glycosylated and packaged into carriers for transport to their final destinations. Two recent...

... fibrosis, ΔF508, is misfolded and retained by ER quality control. As oligosaccharide moieties of glycoproteins are known to mediate interactions with ER lectin chaperones, we investigated the role of N-linked glycosylation in the processing of wild-type and ΔF508 CFTR. We found that N-glycosylation and ER...

... galactosyltransferase (GT) and galactosylhydroxylysyl glucosyltransferase (GGT) activities in vitro. To investigate the in vivo importance of LH3-catalyzed lysine hydroxylation and hydroxylysine-linked glycosylations, three different LH3-manipulated mouse lines were generated. Mice with a mutation that blocked only...

... of posttranslational processing for dystroglycan function. Glycosylation is the crucial modification that modulates the function of dystroglycan as a receptor for extracellular binding partners. It has become clear that perturbation of dystroglycan glycosylation is the central event in the pathogenesis of several...