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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1998-4-10
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pubmed:databankReference |
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pubmed:abstractText |
Tyrosine O-sulfation is a common posttranslational modification of proteins in all multicellular organisms. This reaction is mediated by a Golgi enzyme activity called tyrosylprotein sulfotransferase (TPST) that catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate to tyrosine residues within acidic motifs of polypeptides. Tyrosine O-sulfation has been shown to be important in protein-protein interactions in several systems. For example, sulfation of tyrosine residues in the leukocyte adhesion molecule P-selectin glycoprotein ligand 1 (PSGL-1) is required for binding to P-selectin on activated endothelium. In this report we describe the purification of TPST from rat liver microsomes based on its affinity for the N-terminal 15 amino acids of PSGL-1. We have isolated human and mouse TPST cDNAs that predict type II transmembrane proteins of 370 amino acid residues with almost identical primary structure. The human cDNA encodes a fully functional N-glycosylated enzyme with an apparent molecular mass of approximately 54 kDa when expressed in mammalian cells. This enzyme defines a new class of Golgi sulfotransferases that may catalyze tyrosine O-sulfation of PSGL-1 and other protein substrates involved in diverse physiologic functions including inflammation and hemostasis.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-1379236,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-1554716,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-1601888,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-1718307,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-1898735,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-1942057,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-2168225,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-2295314,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-2341394,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-2434496,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-2447082,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-2910870,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-2919182,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-3121635,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-3768302,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-3782093,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-3862121,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-4381353,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-6180325,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-7559387,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-7585949,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-7585950,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-7629189,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-7721887,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-7947801,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-8033259,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-8117269,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-8530475,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-8617505,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-8618895,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-9015392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-9034160,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-9153262,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-9268297,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-9346953,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501187-9360604
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
95
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2896-901
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9501187-Amino Acid Sequence,
pubmed-meshheading:9501187-Animals,
pubmed-meshheading:9501187-Chromatography, Affinity,
pubmed-meshheading:9501187-Cloning, Molecular,
pubmed-meshheading:9501187-Eukaryotic Cells,
pubmed-meshheading:9501187-Humans,
pubmed-meshheading:9501187-Male,
pubmed-meshheading:9501187-Membrane Glycoproteins,
pubmed-meshheading:9501187-Mice,
pubmed-meshheading:9501187-Microsomes, Liver,
pubmed-meshheading:9501187-Molecular Sequence Data,
pubmed-meshheading:9501187-Phosphoadenosine Phosphosulfate,
pubmed-meshheading:9501187-Protein Binding,
pubmed-meshheading:9501187-Protein Processing, Post-Translational,
pubmed-meshheading:9501187-Rats,
pubmed-meshheading:9501187-Rats, Sprague-Dawley,
pubmed-meshheading:9501187-Recombinant Proteins,
pubmed-meshheading:9501187-Sequence Homology, Amino Acid,
pubmed-meshheading:9501187-Sulfotransferases,
pubmed-meshheading:9501187-Tyrosine
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pubmed:year |
1998
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pubmed:articleTitle |
Tyrosylprotein sulfotransferase: purification and molecular cloning of an enzyme that catalyzes tyrosine O-sulfation, a common posttranslational modification of eukaryotic proteins.
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pubmed:affiliation |
Department of Medicine, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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