Please use this identifier to cite or link to this item:
|Title:||The SXYQRL sequence in the cytoplasmic domain of TGN38 plays a major role in trans-Golgi network localization||Authors:||Wong, S.H.
|Issue Date:||25-Oct-1993||Citation:||Wong, 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.||Abstract:||The 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.||Source Title:||Journal of Biological Chemistry||URI:||http://scholarbank.nus.edu.sg/handle/10635/112135||ISSN:||00219258|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.