Molecular Biology of the Cell Call for Nominations: MBC Editor-in-Chief

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
 QUICK SEARCH:   [advanced]


     


MBC in Press, published online ahead of print October 4, 2006
Mol. Biol. Cell 10.1091/mbc.E06-08-0665

A more recent version of this article appeared on December 1, 2006
This Article
Right arrow Full Text (PDF)
Right arrow Supplemental Materials
Right arrow All Versions of this Article:
E06-08-0665v1
17/12/5153    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Schaub, B. E.
Right arrow Articles by Rohrer, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Schaub, B. E.
Right arrow Articles by Rohrer, J.

Submitted on August 2, 2006
Revised on September 13, 2006
Accepted on September 27, 2006

Transition of Galactosyltransferase 1 from Trans-Golgi Cisterna to the Trans-Golgi Network Is Signal Mediated

Beat E. Schaub, Bea Berger, Eric G. Berger, and Jack Rohrer

Institute of Physiology, University of Zurich, CH-8057 Zurich, Switzerland

Monitoring Editor: Vivek Malhotra

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 {beta}1,4-galactosyltransferase 1 (galT) and {alpha}2,6-sialyltransferase 1 (siaT), two trans-Golgi glycosyltransferases, with respect to their different pathways in monensin treated cells. On 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 video-microscopy as well as Optiprep density gradient fractionation. We show that the first 13 amino acids of the cytoplasmic tail of galT are necessary and sufficient for its localization to swollen vesicles induced by monensin. We also show that the monensin sensitivity resulting from these 13 amino acids can be conferred to siaT, which leads to the rapid accumulation of the galT-siaT chimera in swollen vesicles upon monensin treatment. Based on these data we suggest that cycling between the trans-Golgi cisterna and the trans-Golgi network of galT is signal mediated.


Address correspondence to: Jack Rohrer (rohrer.jack{at}access.unizh.ch)




This article has been cited by other articles:


Home page
Mol. Biol. CellHome page
F. Manolea, A. Claude, J. Chun, J. Rosas, and P. Melancon
Distinct Functions for Arf Guanine Nucleotide Exchange Factors at the Golgi Complex: GBF1 and BIGs Are Required for Assembly and Maintenance of the Golgi Stack and trans-Golgi Network, Respectively
Mol. Biol. Cell, February 1, 2008; 19(2): 523 - 535.
[Abstract] [Full Text] [PDF]




Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2006 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.