| Transition of galactosyltransferase 1 from trans-Golgi cisterna to the trans-Golgi network is signal mediated. | |
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MedLine Citation:
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PMID: 17021253 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Beat E Schaub; Bea Berger; Eric G Berger; Jack Rohrer |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2006-10-04 |
Journal Detail:
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Title: Molecular biology of the cell Volume: 17 ISSN: 1059-1524 ISO Abbreviation: Mol. Biol. Cell Publication Date: 2006 Dec |
Date Detail:
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Created Date: 2006-11-28 Completed Date: 2007-01-23 Revised Date: 2012-01-05 |
Medline Journal Info:
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Nlm Unique ID: 9201390 Medline TA: Mol Biol Cell Country: United States |
Other Details:
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Languages: eng Pagination: 5153-62 Citation Subset: IM |
Affiliation:
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Institute of Physiology, University of Zurich, CH-8057 Zurich, Switzerland. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Brefeldin A / pharmacology Cytoplasmic Vesicles / drug effects Galactosyltransferases / chemistry, metabolism* Green Fluorescent Proteins / metabolism Humans Membrane Glycoproteins / metabolism Membrane Proteins / metabolism Models, Biological Molecular Sequence Data Monensin / pharmacology Mutant Proteins / metabolism Phosphorylation / drug effects Protein Transport / drug effects Recombinant Fusion Proteins / metabolism Sialyltransferases / chemistry, metabolism Signal Transduction* / drug effects trans-Golgi Network / drug effects, metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Membrane Glycoproteins; 0/Membrane Proteins; 0/Mutant Proteins; 0/Recombinant Fusion Proteins; 0/TGOLN2 protein, human; 0/macrogolgin; 147336-22-9/Green Fluorescent Proteins; 17090-79-8/Monensin; 20350-15-6/Brefeldin A; EC 2.4.1.-/Galactosyltransferases; EC 2.4.1.-/beta1,4-galactosyltransferase, human; EC 2.4.99.-/Sialyltransferases; EC 2.4.99.1/beta-D-galactoside alpha 2-6-sialyltransferase |
| Comments/Corrections | |
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