Please use this identifier to cite or link to this item: https://scholarbank.nus.edu.sg/handle/10635/112135
DC FieldValue
dc.titleThe SXYQRL sequence in the cytoplasmic domain of TGN38 plays a major role in trans-Golgi network localization
dc.contributor.authorWong, S.H.
dc.contributor.authorHong, W.
dc.date.accessioned2014-11-28T02:53:36Z
dc.date.available2014-11-28T02:53:36Z
dc.date.issued1993-10-25
dc.identifier.citationWong, S.H.,Hong, W. (1993-10-25). The SXYQRL sequence in the cytoplasmic domain of TGN38 plays a major role in trans-Golgi network localization. Journal of Biological Chemistry 268 (30) : 22853-22862. ScholarBank@NUS Repository.
dc.identifier.issn00219258
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/112135
dc.description.abstractThe trans-Golgi network (TGN) plays a central role in protein sorting/targeting. TGN38 is an integral membrane protein confined mainly to the TGN. When the cytoplasmic 32-residue sequence of TGN38 was fused to the ecto- and transmembrane domains of glycophorin A (a surface protein), the resulting chimeric protein was localized to the TGN. Detailed mutagenesis of the 32-residue sequence revealed that the Ser, Tyr, and Leu residues at positions 23, 25, and 28, respectively, are essential for TGN localization. Further studies demonstrate that the sequence SXYQRL can by itself confer significant TGN localization.
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentINSTITUTE OF MOLECULAR & CELL BIOLOGY
dc.description.sourcetitleJournal of Biological Chemistry
dc.description.volume268
dc.description.issue30
dc.description.page22853-22862
dc.description.codenJBCHA
dc.identifier.isiutNOT_IN_WOS
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