The lectin domains of polypeptide GalNAc-transferases exhibit carbohydrate-binding specificity for GalNAc: lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-O-glycosylation
Identifieur interne : 002B81 ( Main/Exploration ); précédent : 002B80; suivant : 002B82The lectin domains of polypeptide GalNAc-transferases exhibit carbohydrate-binding specificity for GalNAc: lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-O-glycosylation
Auteurs : Hans H. Wandall [Danemark] ; Fernando Irazoqui [Danemark, Argentine] ; Mads Agervig Tarp [Danemark] ; Eric P. Bennett [Danemark] ; Ulla Mandel [Danemark] ; Hideyuki Takeuchi [Japon] ; Kentaro Kato [Danemark] ; Tatsuro Irimura [Japon] ; Ganesh Suryanarayanan [États-Unis] ; Michael A. Hollingsworth [États-Unis] ; Henrik Clausen [Danemark]Source :
- Glycobiology [ 0959-6658 ] ; 2007.
Abstract
Initiation of mucin-type O-glycosylation is controlled by a large family of UDP GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferases). Most GalNAc-transferases contain a ricin-like lectin domain in the C-terminal end, which may confer GalNAc-glycopeptide substrate specificity to the enzyme. We have previously shown that the lectin domain of GalNAc-T4 modulates its substrate specificity to enable unique GalNAc-glycopeptide specificities and that this effect is selectively inhibitable by GalNAc; however, direct evidence of carbohydrate binding of GalNAc-transferase lectins has not been previously presented. Here, we report the direct carbohydrate binding of two GalNAc-transferase lectin domains, GalNAc-T4 and GalNAc-T2, representing isoforms reported to have distinct glycopeptide activity (GalNAc-T4) and isoforms without apparent distinct GalNAc-glycopeptide specificity (GalNAc-T2). Both lectins exhibited specificity for binding of free GalNAc. Kinetic and time-course analysis of GalNAc-T2 demonstrated that the lectin domain did not affect transfer to initial glycosylation sites, but selectively modulated velocity of transfer to subsequent sites and affected the number of acceptor sites utilized. The results suggest that GalNAc-transferase lectins serve to modulate the kinetic properties of the enzymes in the late stages of the initiation process of O-glycosylation to accomplish dense or complete O-glycan occupancy.
Url:
DOI: 10.1093/glycob/cwl082
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: 002719
- to stream Istex, to step Curation: 002719
- to stream Istex, to step Checkpoint: 000834
- to stream Main, to step Merge: 002C07
- to stream Main, to step Curation: 002B81
Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>The lectin domains of polypeptide GalNAc-transferases exhibit carbohydrate-binding specificity for GalNAc: lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-O-glycosylation</title>
<author><name sortKey="Wandall, Hans H" sort="Wandall, Hans H" uniqKey="Wandall H" first="Hans H." last="Wandall">Hans H. Wandall</name>
</author>
<author><name sortKey="Irazoqui, Fernando" sort="Irazoqui, Fernando" uniqKey="Irazoqui F" first="Fernando" last="Irazoqui">Fernando Irazoqui</name>
</author>
<author><name sortKey="Tarp, Mads Agervig" sort="Tarp, Mads Agervig" uniqKey="Tarp M" first="Mads Agervig" last="Tarp">Mads Agervig Tarp</name>
</author>
<author><name sortKey="Bennett, Eric P" sort="Bennett, Eric P" uniqKey="Bennett E" first="Eric P." last="Bennett">Eric P. Bennett</name>
</author>
<author><name sortKey="Mandel, Ulla" sort="Mandel, Ulla" uniqKey="Mandel U" first="Ulla" last="Mandel">Ulla Mandel</name>
</author>
<author><name sortKey="Takeuchi, Hideyuki" sort="Takeuchi, Hideyuki" uniqKey="Takeuchi H" first="Hideyuki" last="Takeuchi">Hideyuki Takeuchi</name>
</author>
<author><name sortKey="Kato, Kentaro" sort="Kato, Kentaro" uniqKey="Kato K" first="Kentaro" last="Kato">Kentaro Kato</name>
</author>
<author><name sortKey="Irimura, Tatsuro" sort="Irimura, Tatsuro" uniqKey="Irimura T" first="Tatsuro" last="Irimura">Tatsuro Irimura</name>
</author>
<author><name sortKey="Suryanarayanan, Ganesh" sort="Suryanarayanan, Ganesh" uniqKey="Suryanarayanan G" first="Ganesh" last="Suryanarayanan">Ganesh Suryanarayanan</name>
</author>
<author><name sortKey="Hollingsworth, Michael A" sort="Hollingsworth, Michael A" uniqKey="Hollingsworth M" first="Michael A." last="Hollingsworth">Michael A. Hollingsworth</name>
</author>
<author><name sortKey="Clausen, Henrik" sort="Clausen, Henrik" uniqKey="Clausen H" first="Henrik" last="Clausen">Henrik Clausen</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">ISTEX</idno>
<idno type="RBID">ISTEX:68A537A80C99C7974AC10794D76F5C4F1BE671D8</idno>
<date when="2007" year="2007">2007</date>
<idno type="doi">10.1093/glycob/cwl082</idno>
<idno type="url">https://api.istex.fr/ark:/67375/HXZ-6R1QHPTW-T/fulltext.pdf</idno>
<idno type="wicri:Area/Istex/Corpus">002719</idno>
<idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">002719</idno>
<idno type="wicri:Area/Istex/Curation">002719</idno>
<idno type="wicri:Area/Istex/Checkpoint">000834</idno>
<idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">000834</idno>
<idno type="wicri:doubleKey">0959-6658:2007:Wandall H:the:lectin:domains</idno>
<idno type="wicri:Area/Main/Merge">002C07</idno>
<idno type="wicri:Area/Main/Curation">002B81</idno>
<idno type="wicri:Area/Main/Exploration">002B81</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title level="a" type="main">The lectin domains of polypeptide GalNAc-transferases exhibit carbohydrate-binding specificity for GalNAc: lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-<hi rend="italic">O</hi>
-glycosylation</title>
<author><name sortKey="Wandall, Hans H" sort="Wandall, Hans H" uniqKey="Wandall H" first="Hans H." last="Wandall">Hans H. Wandall</name>
<affiliation wicri:level="1"><country xml:lang="fr">Danemark</country>
<wicri:regionArea>Department of Medical Biochemistry and Genetics and the Department of Oral Diagnostics, Dental School, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N</wicri:regionArea>
<wicri:noRegion>DK-2200 Copenhagen N</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Irazoqui, Fernando" sort="Irazoqui, Fernando" uniqKey="Irazoqui F" first="Fernando" last="Irazoqui">Fernando Irazoqui</name>
<affiliation wicri:level="1"><country xml:lang="fr">Danemark</country>
<wicri:regionArea>Department of Medical Biochemistry and Genetics and the Department of Oral Diagnostics, Dental School, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N</wicri:regionArea>
<wicri:noRegion>DK-2200 Copenhagen N</wicri:noRegion>
</affiliation>
<affiliation wicri:level="1"><country xml:lang="fr">Argentine</country>
<wicri:regionArea>CIQUIBIC-CONICET/Department of Biological Chemistry, Faculty of Chemical Sciences, National University of Cordoba, 5000 Cordoba</wicri:regionArea>
<wicri:noRegion>5000 Cordoba</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Tarp, Mads Agervig" sort="Tarp, Mads Agervig" uniqKey="Tarp M" first="Mads Agervig" last="Tarp">Mads Agervig Tarp</name>
<affiliation wicri:level="1"><country xml:lang="fr">Danemark</country>
<wicri:regionArea>Department of Medical Biochemistry and Genetics and the Department of Oral Diagnostics, Dental School, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N</wicri:regionArea>
<wicri:noRegion>DK-2200 Copenhagen N</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Bennett, Eric P" sort="Bennett, Eric P" uniqKey="Bennett E" first="Eric P." last="Bennett">Eric P. Bennett</name>
<affiliation wicri:level="1"><country xml:lang="fr">Danemark</country>
<wicri:regionArea>Department of Medical Biochemistry and Genetics and the Department of Oral Diagnostics, Dental School, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N</wicri:regionArea>
<wicri:noRegion>DK-2200 Copenhagen N</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Mandel, Ulla" sort="Mandel, Ulla" uniqKey="Mandel U" first="Ulla" last="Mandel">Ulla Mandel</name>
<affiliation wicri:level="1"><country xml:lang="fr">Danemark</country>
<wicri:regionArea>Department of Medical Biochemistry and Genetics and the Department of Oral Diagnostics, Dental School, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N</wicri:regionArea>
<wicri:noRegion>DK-2200 Copenhagen N</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Takeuchi, Hideyuki" sort="Takeuchi, Hideyuki" uniqKey="Takeuchi H" first="Hideyuki" last="Takeuchi">Hideyuki Takeuchi</name>
<affiliation wicri:level="4"><country xml:lang="fr">Japon</country>
<wicri:regionArea>Laboratory of Cancer Biology and Molecular Immunology, Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033</wicri:regionArea>
<placeName><settlement type="city">Tokyo</settlement>
<region type="région">Région de Kantō</region>
</placeName>
<orgName type="university">Université de Tokyo</orgName>
<placeName><settlement type="city">Tokyo</settlement>
<region type="province">Région de Kantō</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Kato, Kentaro" sort="Kato, Kentaro" uniqKey="Kato K" first="Kentaro" last="Kato">Kentaro Kato</name>
<affiliation wicri:level="1"><country xml:lang="fr">Danemark</country>
<wicri:regionArea>Department of Medical Biochemistry and Genetics and the Department of Oral Diagnostics, Dental School, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N</wicri:regionArea>
<wicri:noRegion>DK-2200 Copenhagen N</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Irimura, Tatsuro" sort="Irimura, Tatsuro" uniqKey="Irimura T" first="Tatsuro" last="Irimura">Tatsuro Irimura</name>
<affiliation wicri:level="4"><country xml:lang="fr">Japon</country>
<wicri:regionArea>Laboratory of Cancer Biology and Molecular Immunology, Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033</wicri:regionArea>
<placeName><settlement type="city">Tokyo</settlement>
<region type="région">Région de Kantō</region>
</placeName>
<orgName type="university">Université de Tokyo</orgName>
<placeName><settlement type="city">Tokyo</settlement>
<region type="province">Région de Kantō</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Suryanarayanan, Ganesh" sort="Suryanarayanan, Ganesh" uniqKey="Suryanarayanan G" first="Ganesh" last="Suryanarayanan">Ganesh Suryanarayanan</name>
<affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Nebraska</region>
</placeName>
<wicri:cityArea>Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Hollingsworth, Michael A" sort="Hollingsworth, Michael A" uniqKey="Hollingsworth M" first="Michael A." last="Hollingsworth">Michael A. Hollingsworth</name>
<affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Nebraska</region>
</placeName>
<wicri:cityArea>Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Clausen, Henrik" sort="Clausen, Henrik" uniqKey="Clausen H" first="Henrik" last="Clausen">Henrik Clausen</name>
<affiliation wicri:level="1"><country xml:lang="fr">Danemark</country>
<wicri:regionArea>Department of Medical Biochemistry and Genetics and the Department of Oral Diagnostics, Dental School, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N</wicri:regionArea>
<wicri:noRegion>DK-2200 Copenhagen N</wicri:noRegion>
</affiliation>
<affiliation wicri:level="1"><country wicri:rule="url">Danemark</country>
</affiliation>
<affiliation wicri:level="1"><country wicri:rule="url">Danemark</country>
</affiliation>
</author>
</analytic>
<monogr></monogr>
<series><title level="j" type="main">Glycobiology</title>
<idno type="ISSN">0959-6658</idno>
<idno type="eISSN">1460-2423</idno>
<imprint><publisher>Oxford University Press</publisher>
<date type="published">2007</date>
<date type="e-published">2007</date>
<biblScope unit="vol">17</biblScope>
<biblScope unit="issue">4</biblScope>
<biblScope unit="page" from="374">374</biblScope>
<biblScope unit="page" to="387">387</biblScope>
</imprint>
<idno type="ISSN">0959-6658</idno>
</series>
</biblStruct>
</sourceDesc>
<seriesStmt><idno type="ISSN">0959-6658</idno>
</seriesStmt>
</fileDesc>
<profileDesc><textClass></textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract">Initiation of mucin-type O-glycosylation is controlled by a large family of UDP GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferases). Most GalNAc-transferases contain a ricin-like lectin domain in the C-terminal end, which may confer GalNAc-glycopeptide substrate specificity to the enzyme. We have previously shown that the lectin domain of GalNAc-T4 modulates its substrate specificity to enable unique GalNAc-glycopeptide specificities and that this effect is selectively inhibitable by GalNAc; however, direct evidence of carbohydrate binding of GalNAc-transferase lectins has not been previously presented. Here, we report the direct carbohydrate binding of two GalNAc-transferase lectin domains, GalNAc-T4 and GalNAc-T2, representing isoforms reported to have distinct glycopeptide activity (GalNAc-T4) and isoforms without apparent distinct GalNAc-glycopeptide specificity (GalNAc-T2). Both lectins exhibited specificity for binding of free GalNAc. Kinetic and time-course analysis of GalNAc-T2 demonstrated that the lectin domain did not affect transfer to initial glycosylation sites, but selectively modulated velocity of transfer to subsequent sites and affected the number of acceptor sites utilized. The results suggest that GalNAc-transferase lectins serve to modulate the kinetic properties of the enzymes in the late stages of the initiation process of O-glycosylation to accomplish dense or complete O-glycan occupancy.</div>
</front>
</TEI>
<affiliations><list><country><li>Argentine</li>
<li>Danemark</li>
<li>Japon</li>
<li>États-Unis</li>
</country>
<region><li>Nebraska</li>
<li>Région de Kantō</li>
</region>
<settlement><li>Tokyo</li>
</settlement>
<orgName><li>Université de Tokyo</li>
</orgName>
</list>
<tree><country name="Danemark"><noRegion><name sortKey="Wandall, Hans H" sort="Wandall, Hans H" uniqKey="Wandall H" first="Hans H." last="Wandall">Hans H. Wandall</name>
</noRegion>
<name sortKey="Bennett, Eric P" sort="Bennett, Eric P" uniqKey="Bennett E" first="Eric P." last="Bennett">Eric P. Bennett</name>
<name sortKey="Clausen, Henrik" sort="Clausen, Henrik" uniqKey="Clausen H" first="Henrik" last="Clausen">Henrik Clausen</name>
<name sortKey="Clausen, Henrik" sort="Clausen, Henrik" uniqKey="Clausen H" first="Henrik" last="Clausen">Henrik Clausen</name>
<name sortKey="Clausen, Henrik" sort="Clausen, Henrik" uniqKey="Clausen H" first="Henrik" last="Clausen">Henrik Clausen</name>
<name sortKey="Irazoqui, Fernando" sort="Irazoqui, Fernando" uniqKey="Irazoqui F" first="Fernando" last="Irazoqui">Fernando Irazoqui</name>
<name sortKey="Kato, Kentaro" sort="Kato, Kentaro" uniqKey="Kato K" first="Kentaro" last="Kato">Kentaro Kato</name>
<name sortKey="Mandel, Ulla" sort="Mandel, Ulla" uniqKey="Mandel U" first="Ulla" last="Mandel">Ulla Mandel</name>
<name sortKey="Tarp, Mads Agervig" sort="Tarp, Mads Agervig" uniqKey="Tarp M" first="Mads Agervig" last="Tarp">Mads Agervig Tarp</name>
</country>
<country name="Argentine"><noRegion><name sortKey="Irazoqui, Fernando" sort="Irazoqui, Fernando" uniqKey="Irazoqui F" first="Fernando" last="Irazoqui">Fernando Irazoqui</name>
</noRegion>
</country>
<country name="Japon"><region name="Région de Kantō"><name sortKey="Takeuchi, Hideyuki" sort="Takeuchi, Hideyuki" uniqKey="Takeuchi H" first="Hideyuki" last="Takeuchi">Hideyuki Takeuchi</name>
</region>
<name sortKey="Irimura, Tatsuro" sort="Irimura, Tatsuro" uniqKey="Irimura T" first="Tatsuro" last="Irimura">Tatsuro Irimura</name>
</country>
<country name="États-Unis"><region name="Nebraska"><name sortKey="Suryanarayanan, Ganesh" sort="Suryanarayanan, Ganesh" uniqKey="Suryanarayanan G" first="Ganesh" last="Suryanarayanan">Ganesh Suryanarayanan</name>
</region>
<name sortKey="Hollingsworth, Michael A" sort="Hollingsworth, Michael A" uniqKey="Hollingsworth M" first="Michael A." last="Hollingsworth">Michael A. Hollingsworth</name>
</country>
</tree>
</affiliations>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002B81 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 002B81 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= MersV1 |flux= Main |étape= Exploration |type= RBID |clé= ISTEX:68A537A80C99C7974AC10794D76F5C4F1BE671D8 |texte= The lectin domains of polypeptide GalNAc-transferases exhibit carbohydrate-binding specificity for GalNAc: lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-O-glycosylation }}
![]() | This area was generated with Dilib version V0.6.33. | ![]() |