Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/112146
Title: Transmembrane topology of the mammalian KDEL receptor
Authors: Singh, P. 
Tang, B.L. 
Wong, S.H. 
Hong, W. 
Issue Date: Oct-1993
Citation: Singh, P.,Tang, B.L.,Wong, S.H.,Hong, W. (1993-10). Transmembrane topology of the mammalian KDEL receptor. Molecular and Cellular Biology 13 (10) : 6435-6441. ScholarBank@NUS Repository.
Abstract: The mammalian KDEL receptor is an integral membrane protein with seven hydrophobic regions. Fusion proteins comprising a 37-kDa N-glycosylation reporter fused downstream of amino-terminal fragments of the KDEL receptor with varying numbers of hydrophobic regions were synthesized in an in vitro translation system containing canine pancreatic microsomes. The luminal or cytosolic orientation of the reporter, and hence of the hydrophilic region to which it is fused, was inferred from the presence or absence of glycosylation, which occurs only in the lumen of the microsomes. The cytosolic orientation of the N and C termini was also confirmed immunocytochemically. Our results suggest that the KDEL receptor is inserted into the membrane with only six transmembrane domains and that both the amino and carboxy termini are located in the cytoplasm.
Source Title: Molecular and Cellular Biology
URI: http://scholarbank.nus.edu.sg/handle/10635/112146
ISSN: 02707306
Appears in Collections:Staff Publications

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