Please use this identifier to cite or link to this item: https://scholarbank.nus.edu.sg/handle/10635/112102
Title: The 17-residue transmembrane domain of β-galactoside α2,6-sialyltransferase is sufficient for golgi retention
Authors: Wong, S.H. 
Low, S.H. 
Hong, W. 
Issue Date: Apr-1992
Citation: Wong, S.H.,Low, S.H.,Hong, W. (1992-04). The 17-residue transmembrane domain of β-galactoside α2,6-sialyltransferase is sufficient for golgi retention. Journal of Cell Biology 117 (2) : 245-258. ScholarBank@NUS Repository.
Abstract: β-Galactoside α2,6-sialyltransferase (ST) is a type II integral membrane protein of the Golgi apparatus involved in the sialylation of N-linked glycans. A series of experiments has shown that the 17-residue transmembrane domain of ST is sufficient to confer localization to the Golgi apparatus when transferred to the corresponding region of a cell surface type II integral membrane protein. Lectin affinity chromatography of chimeric proteins bearing this 17-residue sequence suggests that these chimeric proteins are localized in the trans-Golgi cisternae and/or trans-Golgi network. Further experiments suggest that this 17-residue sequence functions as a retention signal for the Golgi apparatus.
Source Title: Journal of Cell Biology
URI: http://scholarbank.nus.edu.sg/handle/10635/112102
ISSN: 00219525
Appears in Collections:Staff Publications

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