Source:http://linkedlifedata.com/resource/pubmed/id/18346800
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2008-4-8
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pubmed:abstractText |
Nucleotide-sugar transporters (NSTs) transport activated sugars (e.g. UDP-GlcNAc) from the cytosol to the lumen of the endoplasmic reticulum or Golgi apparatus where they are used to make glycoproteins and glycolipids. UDP-Glc is an important component of the N-glycan-dependent quality control (QC) system for protein folding. Because Entamoeba has this QC system while Giardia does not, we hypothesized that transfected Giardia might be used to identify the UDP-Glc transporter of Entamoeba. Here we show Giardia membranes transport UDP-GlcNAc and have apyrases, which hydrolyze nucleoside-diphosphates to make the antiporter nucleoside-monophosphate. The only NST of Giardia (GlNst), which we could identify, transports UDP-GlcNAc in transfected Saccharomyces and is present in perinuclear and peripheral vesicles and increases in expression during encystation. Entamoeba membranes transport three nucleotide-sugars (UDP-Gal, UDP-GlcNAc, and UDP-Glc), and Entamoeba has three NSTs, one of which has been shown previously to transport UDP-Gal (EhNst1). Here we show recombinant EhNst2 transports UDP-Glc in transfected Giardia, while recombinant EhNst3 transports UDP-GlcNAc in transfected Saccharomyces. In summary, all three NSTs of Entamoeba and the single NST of Giardia have been molecularly characterized, and transfected Giardia provides a new system for testing heterologous UDP-Glc transporters.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Apyrase,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleotide Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Uridine Diphosphate...,
http://linkedlifedata.com/resource/pubmed/chemical/Uridine Monophosphate
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0166-6851
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
159
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
44-53
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pubmed:meshHeading |
pubmed-meshheading:18346800-Animals,
pubmed-meshheading:18346800-Apyrase,
pubmed-meshheading:18346800-Biological Transport,
pubmed-meshheading:18346800-Cell Membrane,
pubmed-meshheading:18346800-Entamoeba histolytica,
pubmed-meshheading:18346800-Giardia lamblia,
pubmed-meshheading:18346800-Membrane Transport Proteins,
pubmed-meshheading:18346800-Nucleotide Transport Proteins,
pubmed-meshheading:18346800-Polysaccharides,
pubmed-meshheading:18346800-Protein Folding,
pubmed-meshheading:18346800-Protozoan Proteins,
pubmed-meshheading:18346800-Saccharomyces,
pubmed-meshheading:18346800-Transfection,
pubmed-meshheading:18346800-Uridine Diphosphate N-Acetylglucosamine,
pubmed-meshheading:18346800-Uridine Monophosphate
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pubmed:year |
2008
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pubmed:articleTitle |
Use of Giardia, which appears to have a single nucleotide-sugar transporter for UDP-GlcNAc, to identify the UDP-Glc transporter of Entamoeba.
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pubmed:affiliation |
Department of Molecular and Cell Biology, Boston University Goldman School of Dental Medicine, Boston, MA 02118-2492, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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