Publication type: Article in scientific journal
Type of review: Peer review (publication)
Title: Transition of galactosyltransferase 1 from trans-golgi cisterna to the trans-golgi network is signal mediated
Authors: Schaub, Beat E.
Berger, Bea
Berger, Eric G.
Rohrer, Jack
DOI: 10.1091/mbc.e06-08-0665
Published in: Molecular Biology of the Cell
Volume(Issue): 17
Issue: 12
Pages: 5153
Pages to: 5162
Issue Date: Dec-2006
Publisher / Ed. Institution: American Society for Cell Biology
ISSN: 1939-4586
1059-1524
Language: English
Subject (DDC): 571: Physiology and related subjects
Abstract: The Golgi apparatus (GA) is the organelle where complex glycan formation takes place. In addition, it is a major sorting site for proteins destined for various subcellular compartments or for secretion. Here we investigate beta1,4-galactosyltransferase 1 (galT) and alpha2,6-sialyltransferase 1 (siaT), two trans-Golgi glycosyltransferases, with respect to their different pathways in monensin-treated cells. Upon addition of monensin galT dissociates from siaT and the GA and accumulates in swollen vesicles derived from the trans-Golgi network (TGN), as shown by colocalization with TGN46, a specific TGN marker. We analyzed various chimeric constructs of galT and siaT by confocal fluorescence microscopy and time-lapse videomicroscopy as well as Optiprep density gradient fractionation. We show that the first 13 amino acids of the cytoplasmic tail of galT are necessary for its localization to swollen vesicles induced by monensin. We also show that the monensin sensitivity resulting from the cytoplasmic tail can be conferred to siaT, which leads to the rapid accumulation of the galT-siaT chimera in swollen vesicles upon monensin treatment. On the basis of these data, we suggest that cycling between the trans-Golgi cisterna and the trans-Golgi network of galT is signal mediated.
URI: https://digitalcollection.zhaw.ch/handle/11475/6806
Fulltext version: Published version
License (according to publishing contract): Licence according to publishing contract
Departement: Life Sciences and Facility Management
Organisational Unit: Institute of Chemistry and Biotechnology (ICBT)
Appears in Collections:Publikationen Life Sciences und Facility Management

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