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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
19
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pubmed:dateCreated |
1995-6-15
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pubmed:abstractText |
Syk is a cytoplasmic protein-tyrosine kinase containing two amino-terminal Src homology 2 domains that is activated following ligation of the B cell antigen receptor. Syk activation in B cells correlates with Syk tyrosine phosphorylation as well as with Syk SH2-mediated association with the tyrosine-phosphorylated Ig alpha and Ig beta B cell antigen receptor subunits. Tyrosine-phosphorylated peptide 20-mers representing Ig alpha and Ig beta immunoreceptor tyrosine activation motifs were synthesized and found to stimulate the specific activity of Syk by as much as 10-fold in vitro. Maximal phosphopeptide-induced Syk activation required both Syk SH2 domains and phosphorylation of both tyrosine residues present in the immunoreceptor tyrosine activation motif. The biochemical mechanism responsible for the phosphopeptide-induced Syk enzyme activation appears to be a function of Syk autophosphorylation. Our observations suggest the association of Syk tandem SH2 domains with the tyrosine-phosphorylated Ig alpha and/or Ig beta immunoreceptor tyrosine activation motifs in B cells stimulates Syk autophosphorylation leading to Syk enzyme activation.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, B-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Syk kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11590-4
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:7538118-Amino Acid Sequence,
pubmed-meshheading:7538118-Animals,
pubmed-meshheading:7538118-B-Lymphocytes,
pubmed-meshheading:7538118-Cell Line,
pubmed-meshheading:7538118-Cercopithecus aethiops,
pubmed-meshheading:7538118-Consensus Sequence,
pubmed-meshheading:7538118-Enzyme Activation,
pubmed-meshheading:7538118-Enzyme Precursors,
pubmed-meshheading:7538118-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:7538118-Kinetics,
pubmed-meshheading:7538118-Mice,
pubmed-meshheading:7538118-Molecular Sequence Data,
pubmed-meshheading:7538118-Peptide Fragments,
pubmed-meshheading:7538118-Phosphopeptides,
pubmed-meshheading:7538118-Phosphorylation,
pubmed-meshheading:7538118-Phosphotyrosine,
pubmed-meshheading:7538118-Protein-Tyrosine Kinases,
pubmed-meshheading:7538118-Receptors, Antigen, B-Cell,
pubmed-meshheading:7538118-Signal Transduction,
pubmed-meshheading:7538118-Transfection,
pubmed-meshheading:7538118-Tyrosine
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pubmed:year |
1995
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pubmed:articleTitle |
Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Ig alpha/Ig beta immunoreceptor tyrosine activation motif binding and autophosphorylation.
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pubmed:affiliation |
Department of Molecular Biology, Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, New Jersey 08543, USA.
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pubmed:publicationType |
Journal Article
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