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
ISTEX:38F5B79FADC833554B361885A6814430224A208FLe document en format XML
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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.</abstract><qualityIndicators><score>7.4</score><pdfVersion>1.3</pdfVersion><pdfPageSize>595 x 842 pts (A4)</pdfPageSize><refBibsNative>false</refBibsNative><keywordCount>5</keywordCount><abstractCharCount>1439</abstractCharCount><pdfWordCount>6017</pdfWordCount><pdfWordsPerPage>752</pdfWordsPerPage><pdfCharCount>40906</pdfCharCount><pdfPageCount>8</pdfPageCount><abstractWordCount>200</abstractWordCount><pdfText>true</pdfText></qualityIndicators><title>Protein-specific glycosylation: signal patches and cis-controlling peptidic elements</title><pmid><json:string>19563271</json:string></pmid><genre><json:string>review-article</json:string></genre><host><title>Biological Chemistry</title><language><json:string>unknown</json:string></language><publicationDate>2009</publicationDate><copyrightDate>2009</copyrightDate><issn><json:string>1431-6730</json:string></issn><eissn><json:string>1437-4315</json:string></eissn><publisherId><json:string>bchm</json:string></publisherId><volume>390</volume><issue>7</issue><pages><first>619</first><last>626</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>2009-03-05</json:string><json:string>2009</json:string></date><geogName></geogName><orgName><json:string>University of Cologne</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>R. 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Breloy</json:string></persName><placeName><json:string>Germany</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Colley, 2009</json:string><json:string>Bause and Legler, 1981</json:string><json:string>Sentandreu and Northcote, 1969</json:string><json:string>Do et al., 2000</json:string><json:string>Lee et al., 2007</json:string><json:string>Breloy et al., 2008</json:string><json:string>Skelton et al., 1992</json:string><json:string>Haltiwanger and Stanley, 2002</json:string><json:string>Chen et al., 2001</json:string><json:string>Tarp and Clausen, 2008</json:string><json:string>Lehle et al., 2006</json:string><json:string>Moloney et al., 2000</json:string><json:string>Smalheiser et al., 1998</json:string><json:string>Hildebrandt et al., 2009</json:string><json:string>Hutzler et al., 2007</json:string><json:string>Martinez-Pomares et al., 1999</json:string><json:string>Florea et al., 2006</json:string><json:string>Rampal et al., 2007</json:string><json:string>Cremer et 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2003</json:string><json:string>Kunz et al., 2005</json:string><json:string>Braulke et al., 2008</json:string><json:string>Suzuki et al., 2003</json:string><json:string>Fiete et al., 2007</json:string><json:string>Julenius et al., 2005</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/QT4-NBLDDR8J-7</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - biochemistry & molecular biology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - biochemistry & molecular biology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Clinical Biochemistry</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Molecular 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<ref target="http://www.tei-c.org/">We use TEI</ref></desc></application></appInfo></encodingDesc><profileDesc><abstract><head>Abstract</head><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>-regulatory elements. Another example of such a <hi rend="italic">cis</hi>-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 <hi rend="italic">cis</hi>-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.</p></abstract><textClass ana="subject"><keywords scheme="heading"><term>Protein-specific glycosylation and its control</term></keywords></textClass><textClass ana="keyword"><keywords><term>Fringe</term><term>LacdiNAc</term><term>mannose-6-phosphate</term><term>O-mannosylation</term><term>polysialylation</term></keywords></textClass><langUsage><language ident="EN"></language></langUsage></profileDesc><revisionDesc><change when="2020-03-12" who="#istex" xml:id="pub2tei">formatting</change><change xml:id="refBibs-istex" who="#ISTEX-API" when="2020-04-1">References added</change></revisionDesc></teiHeader></istex:fulltextTEI></fulltext><metadata><istex:metadataXml wicri:clean="corpus degruyter-journals" wicri:toSee="no header"><istex:xmlDeclaration>version="1.0" encoding="UTF-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//Atypon//DTD Atypon Systems Archival NLM DTD Suite v2.2.0 20090301//EN" URI="nlm-dtd/archivearticle.dtd" name="istex:docType"></istex:docType><istex:document><article article-type="review-article" xml:lang="EN"><front><journal-meta><journal-id journal-id-type="publisher-id">bchm</journal-id><abbrev-journal-title abbrev-type="full">Biological Chemistry</abbrev-journal-title><issn pub-type="epub">1437-4315</issn><issn pub-type="ppub">1431-6730</issn><publisher><publisher-name>Walter de Gruyter</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="publisher-id">bc.2009.043</article-id><article-id pub-id-type="doi">10.1515/BC.2009.043</article-id><article-categories><subj-group subj-group-type="heading"><subject>Protein-specific glycosylation and its control</subject></subj-group></article-categories><title-group><article-title>Protein-specific glycosylation: signal patches and <italic>cis</italic>-controlling peptidic elements</article-title></title-group><contrib-group><contrib contrib-type="author"><name name-style="western"><given-names>Franz-Georg</given-names><x> </x><surname>Hanisch</surname></name><xref ref-type="aff" rid="aff1 aff2"><sup>1,2</sup></xref><x>, </x></contrib><contrib contrib-type="author"><name name-style="western"><given-names>Isabelle</given-names><x> </x><surname>Breloy</surname></name><xref ref-type="aff" rid="aff1"><sup>1</sup></xref><x>, </x></contrib><aff id="aff1"><sup>1</sup>Institute of Biochemistry II, Medical Faculty, University of Cologne, Joseph-Stelzmann-Str. 52, D-50931 Köln, Germany</aff><aff id="aff2"><sup>2</sup>Center for Molecular Medicine Cologne, University of Cologne, Robert-Koch-Str. 21, D-50931 Köln, Germany</aff></contrib-group><author-notes><corresp>Corresponding author <email xlink:href="mailto:franz.hanisch@uni-koeln.de">franz.hanisch@uni-koeln.de</email></corresp></author-notes><pub-date pub-type="ppub"><day>01</day><month>07</month><year>2009</year><string-date>July 2009</string-date></pub-date><pub-date pub-type="epub"><day>05</day><month>03</month><year>2009</year></pub-date><volume>390</volume><issue>7</issue><fpage>619</fpage><lpage>626</lpage><history><date date-type="received"><day>22</day><month>12</month><year>2008</year></date><date date-type="accepted"><day>26</day><month>1</month><year>2009</year></date></history><copyright-statement>©2009 by Walter de Gruyter Berlin New York</copyright-statement><copyright-year>2009</copyright-year><related-article related-article-type="pdf" xlink:href="bc.2009.043.pdf"></related-article><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>-regulatory elements. Another example of such a <italic>cis</italic>-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 <italic>cis</italic>-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.</p></abstract><kwd-group><title>Keywords</title><kwd>Fringe</kwd><x>, </x><kwd>LacdiNAc</kwd><x>, </x><kwd>mannose-6-phosphate</kwd><x>, </x><kwd>O-mannosylation</kwd><x>, </x><kwd>polysialylation</kwd></kwd-group><counts><fig-count count="1"></fig-count><table-count count="0"></table-count><ref-count count="67"></ref-count></counts></article-meta></front></article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Protein-specific glycosylation: signal patches and cis-controlling peptidic elements</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Protein-specific glycosylation: signal patches and cis-controlling peptidic elements</title></titleInfo><name type="personal"><namePart type="given">Franz-Georg</namePart><namePart type="family">Hanisch</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Isabelle</namePart><namePart type="family">Breloy</namePart><affiliation>Institute of Biochemistry II, Medical Faculty, University of Cologne, Joseph-Stelzmann-Str. 52, D-50931 Köln, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="review-article" displayLabel="review-article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-L5L7X3NF-P">review-article</genre><originInfo><publisher>Walter de Gruyter</publisher><dateIssued encoding="w3cdtf">2009-07-01</dateIssued><dateCreated encoding="w3cdtf">2009-03-05</dateCreated><copyrightDate encoding="w3cdtf">2009</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><extent unit="figures">1</extent><extent unit="references">67</extent></physicalDescription><abstract 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.</abstract><subject><genre>Keywords</genre><topic>Fringe</topic><topic>LacdiNAc</topic><topic>mannose-6-phosphate</topic><topic>O-mannosylation</topic><topic>polysialylation</topic></subject><relatedItem type="host"><titleInfo><title>Biological Chemistry</title></titleInfo><titleInfo type="abbreviated"><title>Biological Chemistry</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>Walter de Gruyter</publisher><dateIssued encoding="w3cdtf">2009-07-01</dateIssued><dateCreated encoding="w3cdtf">2009-03-05</dateCreated><copyrightDate encoding="w3cdtf">2009</copyrightDate></originInfo><identifier type="ISSN">1431-6730</identifier><identifier type="eISSN">1437-4315</identifier><identifier type="PublisherID">bchm</identifier><part><date>2009</date><detail type="volume"><caption>vol.</caption><number>390</number></detail><detail type="issue"><caption>no.</caption><number>7</number></detail><extent unit="pages"><start>619</start><end>626</end></extent></part></relatedItem><identifier type="istex">38F5B79FADC833554B361885A6814430224A208F</identifier><identifier type="ark">ark:/67375/QT4-NBLDDR8J-7</identifier><identifier type="DOI">10.1515/BC.2009.043</identifier><identifier type="ArticleID">bc.2009.043</identifier><identifier type="pdf">bc.2009.043.pdf</identifier><accessCondition type="use and reproduction" contentType="copyright">©2009 by Walter de Gruyter Berlin New York, 2009</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-B4QPMMZB-D">degruyter-journals</recordContentSource><recordOrigin>Converted from (version 1.2.10) to MODS version 3.6.</recordOrigin><recordCreationDate encoding="w3cdtf">2020-04-03</recordCreationDate></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/QT4-NBLDDR8J-7/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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