Journal article

POSTTRANSLATIONAL MODIFICATIONS DISTINGUISH CELL-SURFACE FROM GOLGI-RETAINED BETA-1,4 GALACTOSYLTRANSFERASE MOLECULES - GOLGI LOCALIZATION INVOLVES ACTIVE RETENTION

RD TEASDALE, F MATHESON, PA GLEESON

Glycobiology | OXFORD UNIV PRESS UNITED KINGDOM | Published : 1994

Abstract

beta 1,4 Galactosyltransferase (GalT) is a membrane-bound enzyme localized predominantly to the trans-Golgi cisternae. Our previous studies have shown that the transmembrane domain of bovine GalT plays a critical role in Golgi localization (Teasdale, R.D., D'Agostaro, G. and Gleeson, P.A., J. Biol. Chem., 267, 4084-4096, 1992). Here we have compared the localization and post-translational modifications of full-length bovine GalT with a GalT/hybrid molecule where the transmembrane domain of GalT was replaced with that of the transferrin receptor. GalT/hybrid molecules were expressed on the surface of transfected cells; however, differences were observed in the distribution of the hybrid molec..

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