Please use this identifier to cite or link to this item: https://scholarbank.nus.edu.sg/handle/10635/111872
Title: Endoplasmic reticulum retention mediated by the transmembrane domain of type II membrane proteins Sec12p and glucosidase 1
Authors: Tang, B.L. 
Low, S.H.
Hong, W. 
Keywords: Endoplasmic reticulum
Golgi apparatus
Retention
Type II protein
Issue Date: Jun-1997
Citation: Tang, B.L.,Low, S.H.,Hong, W. (1997-06). Endoplasmic reticulum retention mediated by the transmembrane domain of type II membrane proteins Sec12p and glucosidase 1. European Journal of Cell Biology 73 (2) : 98-104. ScholarBank@NUS Repository.
Abstract: The yeast Sec12p, a type II protein localized to the yeast endoplasmic reticulum (ER), is similarly localized to the ER when expressed in mammalian cells. Replacing the transmembrane domain of the plasma membrane molecule dipeptidyl peptidase IV (D4) with that of Sec12p or the ER-localized enzyme glucosidase 1 resulted in the ER retention of the chimeric molecules, as assessed by immunocytochemical localization and the persistence of pulse-labeled proteins in the endoglycosidase H-sensitive form. Retention is not due to gross misfolding as these chimeras remained enzymatically active. Density gradient analysis revealed that the ER-localized chimeric molecules form high molecular weight oligomers quickly after synthesis. The type II transmembrane domain of ER proteins could therefore mediate retention in the ER.
Source Title: European Journal of Cell Biology
URI: http://scholarbank.nus.edu.sg/handle/10635/111872
ISSN: 01719335
Appears in Collections:Staff Publications

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