dc.creator | Lorenz, Virginia | |
dc.creator | Ditamo, Yanina | |
dc.creator | Cejas, Romina Beatríz | |
dc.creator | Carrizo Garcia, Maria Elena | |
dc.creator | Bennett, Eric P. | |
dc.creator | Clausen, Henrik | |
dc.creator | Nores, Gustavo Alejandro | |
dc.creator | Irazoqui, Fernando Jose | |
dc.date.accessioned | 2018-08-28T18:23:30Z | |
dc.date.accessioned | 2018-11-06T15:03:38Z | |
dc.date.available | 2018-08-28T18:23:30Z | |
dc.date.available | 2018-11-06T15:03:38Z | |
dc.date.created | 2018-08-28T18:23:30Z | |
dc.date.issued | 2016-12 | |
dc.identifier | Lorenz, Virginia; Ditamo, Yanina; Cejas, Romina Beatríz; Carrizo Garcia, Maria Elena; Bennett, Eric P.; et al.; Extrinsic functions of lectin domains in O-N-acetylgalactosamine glycan biosynthesis; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 291; 49; 12-2016; 25339-25350 | |
dc.identifier | 0021-9258 | |
dc.identifier | http://hdl.handle.net/11336/57375 | |
dc.identifier | 1083-351X | |
dc.identifier | CONICET Digital | |
dc.identifier | CONICET | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1893349 | |
dc.description.abstract | Glycan biosynthesis occurs mainly in Golgi. Molecular organization and functional regulation of this process are not well understood. We evaluated the extrinsic effect of lectin domains (β-trefoil fold) of polypeptide GalNAc-transferases (ppGalNAc-Ts) on catalytic activity of glycosyltransferases during O-GalNAc glycan biosynthesis. The presence of lectin domain T3lec or T4lec during ppGalNAc-T2 and ppGalNAc-T3 catalytic reaction had a clear inhibitory effect on GalNAc-T activity. Interaction of T3lec or T4lec with ppGalNAc-T2 catalytic domain was not mediated by carbohydrate. T3lec, but not T2lec and T4lec, had a clear activating effect on Drosophila melanogaster core 1 galactosyltransferase enzyme activity and a predominant inhibitory effect on in vivo human core 1 glycan biosynthesis. The regulatory role of the β-trefoil fold of ppGalNAc-Ts in enzymatic activity of glycosyltransferases involved in the O-glycan biosynthesis pathway, described here for the first time, helps clarify the mechanism of biosynthesis of complex biopolymers (such as glycans) that is not template-driven. | |
dc.language | eng | |
dc.publisher | American Society for Biochemistry and Molecular Biology | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1074/jbc.M116.740795 | |
dc.relation | info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/291/49/25339 | |
dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.subject | GLYCOBIOLOGY | |
dc.subject | GLYCOPROTEIN BIOSYNTHESIS | |
dc.subject | GLYCOSYLATION INHIBITOR | |
dc.subject | LECTIN | |
dc.subject | MUCIN | |
dc.title | Extrinsic functions of lectin domains in O-N-acetylgalactosamine glycan biosynthesis | |
dc.type | Artículos de revistas | |
dc.type | Artículos de revistas | |
dc.type | Artículos de revistas | |