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The EXT1/EXT2 tumor suppressors: catalytic activities and role in heparan sulfate biosynthesis
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
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2000 (English)In: EMBO Reports, ISSN 1469-221X, E-ISSN 1469-3178, Vol. 1, no 3, 282-286 p.Article in journal (Refereed) Published
Abstract [en]

The D-glucuronyltransferase and N-acetyl-D-glucosaminyltransferase reactions in heparan sulfate biosynthesis have been associated with two genes, EXT1 and EXT2, which are also implicated in the inherited bone disorder, multiple exostoses. Since the cell systems used to express recombinant EXT proteins synthesize endogenous heparan sulfate, and the EXT proteins tend to associate, it has not been possible to define the functional roles of the individual protein species. We therefore expressed EXT1 and EXT2 in yeast, which does not synthesize heparan sulfate. The recombinant EXT1 and EXT2 were both found to catalyze both glycosyltransferase reactions in vitro. Coexpression of the two proteins, but not mixing of separately expressed recombinant EXT1 and EXT2, yields hetero-oligomeric complexes in yeast and mammalian cells, with augmented glycosyltransferase activities. This stimulation does not depend on the membrane-bound state of the proteins.

Place, publisher, year, edition, pages
2000. Vol. 1, no 3, 282-286 p.
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Medical and Health Sciences
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URN: urn:nbn:se:uu:diva-133863DOI: 10.1093/embo-reports/kvd045PubMedID: 11256613OAI: oai:DiVA.org:uu-133863DiVA: diva2:370465
Available from: 2010-11-16 Created: 2010-11-16 Last updated: 2017-12-12Bibliographically approved

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Lidholt, Kerstin

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