000087545 001__ 87545 000087545 005__ 20200716101509.0 000087545 0247_ $$2doi$$a10.1016/j.sbi.2018.12.007 000087545 0248_ $$2sideral$$a110346 000087545 037__ $$aART-2019-110346 000087545 041__ $$aeng 000087545 100__ $$0(orcid)0000-0002-1924-334X$$ade las Rivas, M. 000087545 245__ $$aPolypeptide GalNAc-Ts: from redundancy to specificity 000087545 260__ $$c2019 000087545 5060_ $$aAccess copy available to the general public$$fUnrestricted 000087545 5203_ $$aMucin-type O-glycosylation is a post-translational modification (PTM) that is predicted to occur in more than the 80% of the proteins that pass through the Golgi apparatus. This PTM is initiated by a family of polypeptide GalNAc-transferases (GalNAc-Ts) that modify Ser and Thr residues of proteins through the addition of a GalNAc moiety. These enzymes are type II membrane proteins that consist of a Golgi luminal catalytic domain connected by a flexible linker to a ricin type lectin domain. Together, both domains account for the different glycosylation preferences observed among isoenzymes. Although it is well accepted that most of the family members share some degree of redundancy toward their protein and glycoprotein substrates, it has been recently found that several GalNAc-Ts also possess activity toward specific targets. Despite the high similarity between isoenzymes, structural differences have recently been reported that are key to understanding the molecular basis of both their redundancy and specificity. The present review focuses on the molecular aspects of the protein substrate recognition and the different glycosylation preferences of these enzymes, which in turn will serve as a roadmap to the rational design of specific modulators of mucin-type O-glycosylation. 000087545 536__ $$9info:eu-repo/grantAgreement/ES/DGA/E34-R17$$9info:eu-repo/grantAgreement/EC/FP7/283570/EU/Transnational access and enhancement of integrated Biological Structure determination at synchrotron X-ray radiation facilities/BIOSTRUCT-X$$9info:eu-repo/grantAgreement/ES/MEC/BFU2016-75633-P$$9info:eu-repo/grantAgreement/ES/MEC/CTQ2013-44367-C2-2-P 000087545 540__ $$9info:eu-repo/semantics/openAccess$$aAll rights reserved$$uhttp://www.europeana.eu/rights/rr-f/ 000087545 590__ $$a6.908$$b2019 000087545 591__ $$aCELL BIOLOGY$$b36 / 195 = 0.185$$c2019$$dQ1$$eT1 000087545 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b36 / 297 = 0.121$$c2019$$dQ1$$eT1 000087545 592__ $$a4.07$$b2019 000087545 593__ $$aStructural Biology$$c2019$$dQ1 000087545 593__ $$aMolecular Biology$$c2019$$dQ1 000087545 655_4 $$ainfo:eu-repo/semantics/review$$vinfo:eu-repo/semantics/acceptedVersion 000087545 700__ $$aLira-Navarrete, E. 000087545 700__ $$aGerken, T.A. 000087545 700__ $$0(orcid)0000-0002-3122-9401$$aHurtado-Guerrero, R.$$uUniversidad de Zaragoza 000087545 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole. 000087545 773__ $$g56 (2019), 87-96$$pCurr. opin. struck. biol.$$tCurrent Opinion in Structural Biology$$x0959-440X 000087545 8564_ $$s588915$$uhttps://zaguan.unizar.es/record/87545/files/texto_completo.pdf$$yPostprint 000087545 8564_ $$s56515$$uhttps://zaguan.unizar.es/record/87545/files/texto_completo.jpg?subformat=icon$$xicon$$yPostprint 000087545 909CO $$ooai:zaguan.unizar.es:87545$$particulos$$pdriver 000087545 951__ $$a2020-07-16-09:18:02 000087545 980__ $$aARTICLE