Please use this identifier to cite or link to this item: https://scholarbank.nus.edu.sg/handle/10635/112136
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dc.titleThe transmembrane domain of N-glucosaminyltransferase I contains a Golgi retention signal
dc.contributor.authorTang, B.L.
dc.contributor.authorWong, S.H.
dc.contributor.authorLow, S.H.
dc.contributor.authorHong, W.
dc.date.accessioned2014-11-28T02:53:36Z
dc.date.available2014-11-28T02:53:36Z
dc.date.issued1992-05-15
dc.identifier.citationTang, B.L.,Wong, S.H.,Low, S.H.,Hong, W. (1992-05-15). The transmembrane domain of N-glucosaminyltransferase I contains a Golgi retention signal. Journal of Biological Chemistry 267 (14) : 10122-10126. ScholarBank@NUS Repository.
dc.identifier.issn00219258
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/112136
dc.description.abstractThe enzyme N-acetylglucosaminyltransferase I (NT, EC 2.4.1.101) is a resident type II transmembrane protein of the Golgi apparatus. To delineate the portion of its primary sequence that is responsible for the Golgi retention of this protein, we constructed chimeras containing different N-terminal portions of NT joined to a reporter sequence, the ectodomain of a type II surface membrane protein. These chimeric proteins were found to be retained in the Golgi apparatus as assessed by cell surface biotinylation and immunofluorescence. We found that the transmembrane domain of NT is sufficient to confer Golgi retention of the fusion proteins and propose that it contains the Golgi retention signal of the parent molecule.
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentINSTITUTE OF MOLECULAR & CELL BIOLOGY
dc.description.sourcetitleJournal of Biological Chemistry
dc.description.volume267
dc.description.issue14
dc.description.page10122-10126
dc.description.codenJBCHA
dc.identifier.isiutNOT_IN_WOS
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