Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/10757
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dc.contributor.authorChristiansen, Daleen
dc.contributor.authorMilland, Julieen
dc.contributor.authorDodson, Hayley Cen
dc.contributor.authorLazarus, Brooke Den
dc.contributor.authorSandrin, Mauro Sen
dc.date.accessioned2015-05-16T00:18:26Z
dc.date.available2015-05-16T00:18:26Z
dc.date.issued2009-05-06en
dc.identifier.citationJournal of Molecular Recognition : Jmr; 22(3): 250-4en
dc.identifier.govdoc19165762en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/10757en
dc.description.abstractCarbohydrate structures influence many aspects of cell biology. Manipulating the glycosyltransferase enzymes, that sequentially add carbohydrate moieties to proteins and lipids as they pass through the Golgi and secretory pathway, can alter these carbohydrate epitopes. We previously demonstrated that the eight amino acid cytoplasmic tail of alpha1,2fucosyltransferase (FT) contained a sequence for Golgi localisation. In this study, we examined the localisation of the closely related secretor type alpha1,2fucosyltransferase (Sec) which has a smaller, yet apparently unrelated, five amino acid cytoplasmic tail. In contrast to the Golgi localisation of FT, Sec displayed atypical cytoplasmic vesicular-like staining. However, replacing just the five amino acid tail of Sec with FT was sufficient to relocalise the enzyme to a perinuclear region with Golgi-like staining. The biological significance of this relocalisation was this chimaeric enzyme was more effective than FT at competing for N-Acetyl-lactosamine and thus was superior in reducing expression of the Galalpha(1,3)Gal xenoepitope.en
dc.language.isoenen
dc.subject.otherAnimalsen
dc.subject.otherCell Lineen
dc.subject.otherCytoplasm.enzymologyen
dc.subject.otherFucosyltransferases.chemistry.metabolismen
dc.subject.otherGolgi Apparatus.enzymologyen
dc.subject.otherMutant Proteins.metabolismen
dc.subject.otherProtein Structure, Tertiaryen
dc.subject.otherProtein Transporten
dc.subject.otherRecombinant Fusion Proteins.metabolismen
dc.subject.otherStructure-Activity Relationshipen
dc.titleThe cytoplasmic and transmembrane domains of secretor type alpha1,2fucosyltransferase confer atypical cellular localisation.en
dc.typeJournal Articleen
dc.identifier.journaltitleJournal of molecular recognition : JMRen
dc.identifier.affiliationDepartment of Surgery, The University of Melbourne, Austin Health/Northern Health, Heidelberg, Victoria 3084, Australiaen
dc.identifier.doi10.1002/jmr.939en
dc.description.pages250-4en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/19165762en
dc.type.austinJournal Articleen
item.grantfulltextnone-
item.cerifentitytypePublications-
item.fulltextNo Fulltext-
item.openairetypeJournal Article-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.languageiso639-1en-
crisitem.author.deptSurgery (University of Melbourne)-
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