Source:http://linkedlifedata.com/resource/pubmed/id/16859706
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
2006-8-1
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| pubmed:abstractText |
TPST1 is a human tyrosylprotein sulfotransferase that uses 3'phosphoadenosine-5'phosphosulfate (PAPS) to transfer the sulfate moiety to proteins predominantly designated for secretion. To achieve a general understanding of the cellular role of human tyrosine-directed sulfotransferases, we investigated targeting, structure and posttranslational modification of TPST1. Golgi localisation of the enzyme in COS-7 and HeLa cells was visualised by fluorescence imaging techniques. PNGase treatment and mutational studies determined that TPST1 bears N-linked glycosyl residues exclusively at position Asn60 and Asn262. By alanine mutation of these asparagine residues, we could determine that the N-linked oligosaccharides do not have an influence on Golgi retention of TPST1. In concert with N and C-terminal flanking residues, the transmembrane domain of TPST1 was determined to act in targeting and retention of the enzyme to the trans-Golgi compartment. This domain exhibits a pronounced secondary structure in a lipid environment. Further in vivo FRET studies using the transmembrane domain suggest that the human tyrosylprotein sulfotransferase may be functional as homodimer/oligomer in the trans-Golgi compartment.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Asparagine,
http://linkedlifedata.com/resource/pubmed/chemical/Autoantigens,
http://linkedlifedata.com/resource/pubmed/chemical/Golgi complex autoantigen, 97-kDa,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfotransferases,
http://linkedlifedata.com/resource/pubmed/chemical/protein-tyrosine sulfotransferase
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| pubmed:status |
MEDLINE
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| pubmed:month |
Aug
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| pubmed:issn |
0022-2836
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
18
|
| pubmed:volume |
361
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
436-49
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:16859706-Amino Acid Sequence,
pubmed-meshheading:16859706-Animals,
pubmed-meshheading:16859706-Asparagine,
pubmed-meshheading:16859706-Autoantigens,
pubmed-meshheading:16859706-COS Cells,
pubmed-meshheading:16859706-Cercopithecus aethiops,
pubmed-meshheading:16859706-Dimerization,
pubmed-meshheading:16859706-Fluorescence Resonance Energy Transfer,
pubmed-meshheading:16859706-Glycosylation,
pubmed-meshheading:16859706-Golgi Apparatus,
pubmed-meshheading:16859706-HeLa Cells,
pubmed-meshheading:16859706-Humans,
pubmed-meshheading:16859706-Intracellular Membranes,
pubmed-meshheading:16859706-Molecular Sequence Data,
pubmed-meshheading:16859706-Mutation,
pubmed-meshheading:16859706-Oligosaccharides,
pubmed-meshheading:16859706-Protein Binding,
pubmed-meshheading:16859706-Protein Processing, Post-Translational,
pubmed-meshheading:16859706-Protein Structure, Tertiary,
pubmed-meshheading:16859706-Sulfotransferases
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| pubmed:year |
2006
|
| pubmed:articleTitle |
Human TPST1 transmembrane domain triggers enzyme dimerisation and localisation to the Golgi compartment.
|
| pubmed:affiliation |
Department of Structural and Medicinal Biochemistry, University of Duisburg-Essen and Centre for Medicinal Biotechnology, Universitätsstr. 2-5, 45117 Essen, Germany.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|