Protein-specific glycosylation: signal patches and cis-controlling peptidic elements
Identifieur interne : 001865 ( Istex/Corpus ); précédent : 001864; suivant : 001866Protein-specific glycosylation: signal patches and cis-controlling peptidic elements
Auteurs : Franz-Georg Hanisch ; Isabelle BreloySource :
- Biological Chemistry [ 1431-6730 ] ; 2009.
English descriptors
- Teeft :
- Acceptor site, Acid residues, Acidic surface patch, Adhesion, Amino, Amino acid, Amino acids, Baenziger, Biol, Brain development, Breloy, Carbonic anhydrase, Cellular receptor, Chem, Consensus sequence, Current state, Determinant, Double control, Endo, Enzymatic activity, First fibronectin type, Functional implications, Gamete binding, Glycans, Glycoprotein, Glycosylation, Glycosylation variant, Haltiwanger, Higher level, Human zona pellucida, Hydrolases, Igg2 light chain, Lacdinac, Local peptide environment, Lunatic fringe, Lysosomal, Lysosomal hydrolases, Mammalian glycoproteins, Manic fringe, Mannose, Mannose phosphorylation, Mass spectrometry, Modification, Mouse dnase, Mouse notch1, Mucin, Mucin domain, Ncam, Ncam functions, Neural cell adhesion molecule, Notch receptors, Oligosaccharide, Peptide, Peptide sequence, Peptide stretch, Peptidic elements, Peripheral modification, Polysialic, Polysialic acid, Polysialylation, Proof glycosylation, Protein glycosylation, Protein mannosyltransferases, Protein modification, Protein specificity, Putative glycosylation site, Radical fringe, Receptor, Recognition determinants, Same glycoprotein, Structural analysis, Structural features, Structural properties, Structural studies, Substrate position, Substrate positions, Substrate sites, Target protein, Yeast cells.
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.
Url:
DOI: 10.1515/BC.2009.043
Links to Exploration step
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<front><div type="abstract" xml:lang="en">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.</div>
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<p>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 <hi rend="italic">cis</hi>
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<abstract><title>Abstract</title>
<p>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 <italic>cis</italic>
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