Source:http://linkedlifedata.com/resource/pubmed/id/16009340
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2005-7-22
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pubmed:abstractText |
Protein kinase C (PKC) is a family of serine/threonine kinases whose activity is controlled, in part, by phosphorylation on three conserved residues that are located on the catalytic domain of the enzyme, known as the activation-loop, the turn-motif, and the C-terminal hydrophobic-motif sites. Using a panel of phospho-specific antibodies, we have determined that PKC beta(I) and delta are constitutively phosphorylated on all three sites in unstimulated and activated T cells. Although PKC theta is constitutively phosphorylated at the activation-loop and turn-motif sites in T cells, PMA or anti-CD3/CD28 stimulation results in an increase in phosphorylation at the hydrophobic-motif (Ser695), an event that coincides with translocation of the enzyme from the cytosol/cytoskeleton to the membrane. Studies on the stimulus-induced phosphorylation of PKC theta demonstrate that an upstream kinase activity involving a conventional PKC isoform(s) and the PI3-kinase pathway, rather than autophosphorylation or the rapamycin-sensitive mTOR pathway, regulates this site in T lymphocytes. However, hydrophobic-motif phosphorylation does not appear to control membrane translocation, suggesting that this site may control other aspects of PKC theta signalling.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
334
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
619-30
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:16009340-Amino Acid Motifs,
pubmed-meshheading:16009340-Binding Sites,
pubmed-meshheading:16009340-Humans,
pubmed-meshheading:16009340-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:16009340-Jurkat Cells,
pubmed-meshheading:16009340-Lymphocyte Activation,
pubmed-meshheading:16009340-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:16009340-Phosphorylation,
pubmed-meshheading:16009340-Protein Binding,
pubmed-meshheading:16009340-Protein Kinase C
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pubmed:year |
2005
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pubmed:articleTitle |
Stimulus-induced phosphorylation of PKC theta at the C-terminal hydrophobic-motif in human T lymphocytes.
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pubmed:affiliation |
Department of Biochemistry, Royal College of Surgeons in Ireland, 123 St. Stephens Green, Dublin 2, Ireland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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