Document Detail


Transition of galactosyltransferase 1 from trans-Golgi cisterna to the trans-Golgi network is signal mediated.
MedLine Citation:
PMID:  17021253     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Beat E Schaub; Bea Berger; Eric G Berger; Jack Rohrer
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-10-04
Journal Detail:
Title:  Molecular biology of the cell     Volume:  17     ISSN:  1059-1524     ISO Abbreviation:  Mol. Biol. Cell     Publication Date:  2006 Dec 
Date Detail:
Created Date:  2006-11-28     Completed Date:  2007-01-23     Revised Date:  2012-01-05    
Medline Journal Info:
Nlm Unique ID:  9201390     Medline TA:  Mol Biol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  5153-62     Citation Subset:  IM    
Affiliation:
Institute of Physiology, University of Zurich, CH-8057 Zurich, Switzerland.
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MeSH Terms
Descriptor/Qualifier:
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:
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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