Please use this identifier to cite or link to this item: https://scholarbank.nus.edu.sg/handle/10635/111812
Title: Cell type differences in Golgi retention signals for transmembrane proteins
Authors: Tang, B.L. 
Low, S.H. 
Wong, S.H. 
Hong, W. 
Keywords: CHO cells
Golgi retention
Lysosome
Issue Date: 1995
Citation: Tang, B.L.,Low, S.H.,Wong, S.H.,Hong, W. (1995). Cell type differences in Golgi retention signals for transmembrane proteins. European Journal of Cell Biology 66 (4) : 365-374. ScholarBank@NUS Repository.
Abstract: The transmembrane domain of Golgi resident proteins such as β-galactoside α2,6-sialyltransferase (ST) and N-acetylglucosaminyltransferase 1 (NT) contain a Golgi retention signal which confers Golgi retention to reporter proteins appended to them in the appropriate context. Thus, chimeras of the cell surface protein dipeptidyl peptidase IV containing the transmembrane domain of ST and NT are retained in the Golgi apparatus in MDCK and COS cells, as assessed by indirect immunofluorescence microscopy. Transfection of these chimeric constructs into CHO cells, however, results in their transport to vesicular structures which do not colocalize with that of an endogenous Golgi marker, mannosidase II. Furthermore, the staining pattern of these structures are not affected by brefeldin A. Biochemical analysis of the transgene products in pulse-chase experiments revealed that the chimeric proteins eventually become resistant to endoglycosidase H, suggesting that they are transported beyond the medial Golgi and therefore the vesicular structures are likely to be post-Golgi. The vesicular structures colocalized well with a lysosomal marker, cathepsin D, and also with internalized FITC-dextran chased into the lysosomal compartment. Monitoring the cell surface appearance of the chimeric protein suggests that the majority is transported directly to the lysosomal compartment. Golgi retention can be completely restored for ST and improved for NT by the inclusion of sequences flanking the transmembrane domain. Our results reflect cell type differences in the interpretation of the transmembrane domain Golgi retention signal, established that general Golgi retention of type II glycosyltransferases requires the hydrophilic flanking sequence as well as the transmembrane domain, and demonstrate that proteins which escape Golgi retention may be channeled to the lysosomal pathway.
Source Title: European Journal of Cell Biology
URI: http://scholarbank.nus.edu.sg/handle/10635/111812
ISSN: 01719335
Appears in Collections:Staff Publications

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