Protein-specific glycosylation: signal patches and cis-controlling peptidic elements
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Franz-Georg Hanisch
Abstract
The term ‘protein-specific glycosylation’ refers to important functional implications of a subset of glycosylation types that are under direct control of recognition determinants on the protein. Examples of the latter are found in the formation of the mannose-6-phosphate receptor ligand on lysosomal hydrolases, and in polysialylation of NCAM, which are regulated via conformational signal patches on the protein. Distinct from these examples, the β4-GalNAc modification of N-linked glycans on a selected panel of proteins, such as carbonic anhydrase or glycodelin, was demonstrated recently to require specific protein (sequence) determinants proximal to the glycosylation site that function as cis-regulatory elements. Another example of such a cis-regulatory element was described for the control of mammalian O-mannosylation. In this case, the structural features of substrate sites within the mucin domain of α-dystroglycan are necessary, but not sufficient for determining the transfer of mannose to Ser/Thr. Evidence has been provided that an upstream-located peptide is also essential. Such cis-controlling elements provide a higher level of protein specificity, because a putative glycosylation site cannot result from a single point mutation. Here, we highlight recent work on protein-specific glycosylation with particular emphasis on the above-cited examples and we will try to link protein-specific glycosylation to function.
©2009 by Walter de Gruyter Berlin New York
Articles in the same Issue
- Guest Editorial
- Highlight: Perspectives in glycobiology
- Cell biology and glycosylation: protein targeting by O- and N-linked glycosylation
- Glycosylation- and phosphorylation-dependent intracellular transport of lysosomal hydrolases
- Glycosylation pattern of brush border-associated glycoproteins in enterocyte-like cells: involvement of complex-type N-glycans in apical trafficking
- Impact of glycosylation and detergent-resistant membranes on the function of intestinal sucrase-isomaltase
- MUC1 traverses apical recycling endosomes along the biosynthetic pathway in polarized MDCK cells
- Cell biology and glycosylation: carbohydrate-mediated recognition and signaling in cell proliferation and differentiation
- From structural to functional glycomics: core substitutions as molecular switches for shape and lectin affinity of N-glycans
- Brain development needs sugar: the role of polysialic acid in controlling NCAM functions
- Beyond glycosylation: sialic acid precursors act as signaling molecules and are involved in cellular control of differentiation of PC12 cells
- Glycosylation and disease
- Management of the human mucosal defensive barrier: evidence for glycan legislation
- Regulation and pathophysiological implications of UDP-GlcNAc 2-epimerase/ManNAc kinase (GNE) as the key enzyme of sialic acid biosynthesis
- GD3 synthase overexpression enhances proliferation and migration of MDA-MB-231 breast cancer cells
- Tumor-associated MUC1 glycopeptide epitopes are not subject to self-tolerance and improve responses to MUC1 peptide epitopes in MUC1 transgenic mice
- Protein-specific glycosylation and its control
- Protein-specific glycosylation: signal patches and cis-controlling peptidic elements
- O-glycosylation pattern of CD24 from mouse brain
- Advancements in analytical techniques
- Carbohydrate microarrays: key developments in glycobiology
- On-line nano-HPLC/ESI QTOF MS monitoring of α2–3 and α2–6 sialylation in granulocyte glycosphingolipidome
Articles in the same Issue
- Guest Editorial
- Highlight: Perspectives in glycobiology
- Cell biology and glycosylation: protein targeting by O- and N-linked glycosylation
- Glycosylation- and phosphorylation-dependent intracellular transport of lysosomal hydrolases
- Glycosylation pattern of brush border-associated glycoproteins in enterocyte-like cells: involvement of complex-type N-glycans in apical trafficking
- Impact of glycosylation and detergent-resistant membranes on the function of intestinal sucrase-isomaltase
- MUC1 traverses apical recycling endosomes along the biosynthetic pathway in polarized MDCK cells
- Cell biology and glycosylation: carbohydrate-mediated recognition and signaling in cell proliferation and differentiation
- From structural to functional glycomics: core substitutions as molecular switches for shape and lectin affinity of N-glycans
- Brain development needs sugar: the role of polysialic acid in controlling NCAM functions
- Beyond glycosylation: sialic acid precursors act as signaling molecules and are involved in cellular control of differentiation of PC12 cells
- Glycosylation and disease
- Management of the human mucosal defensive barrier: evidence for glycan legislation
- Regulation and pathophysiological implications of UDP-GlcNAc 2-epimerase/ManNAc kinase (GNE) as the key enzyme of sialic acid biosynthesis
- GD3 synthase overexpression enhances proliferation and migration of MDA-MB-231 breast cancer cells
- Tumor-associated MUC1 glycopeptide epitopes are not subject to self-tolerance and improve responses to MUC1 peptide epitopes in MUC1 transgenic mice
- Protein-specific glycosylation and its control
- Protein-specific glycosylation: signal patches and cis-controlling peptidic elements
- O-glycosylation pattern of CD24 from mouse brain
- Advancements in analytical techniques
- Carbohydrate microarrays: key developments in glycobiology
- On-line nano-HPLC/ESI QTOF MS monitoring of α2–3 and α2–6 sialylation in granulocyte glycosphingolipidome
