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rdf:type |
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lifeskim:mentions |
umls-concept:C0007634,
umls-concept:C0033640,
umls-concept:C0061928,
umls-concept:C0205087,
umls-concept:C0332120,
umls-concept:C0442043,
umls-concept:C1323803,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1710082,
umls-concept:C1879547
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pubmed:issue |
Pt 2
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pubmed:dateCreated |
2001-8-21
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pubmed:abstractText |
At least two signalling systems have the potential to contribute to the activation of protein kinase C (PKC) family members such as PKCepsilon. One of these is phosphoinositide 3-kinase (PI 3-kinase), whose lipid products activate PKCepsilon in vitro and in living cells. The recent observation that there are multiple waves of PI 3-kinase and PKCepsilon activity within the G(0)-to-S phase interval provides a new opportunity to investigate the relationship between these two signalling enzymes in vivo. We have assessed the relative importance of the early and late waves of PI 3-kinase activity for the corresponding waves of PKCepsilon activity. Blocking the first phase of PI 3-kinase activity inhibited both early and late activation of PKCepsilon. In contrast, the second wave of PI 3-kinase activity was dispensable for late activation of PKCepsilon. These findings suggested that early PI 3-kinase activation induced a stable change in PKCepsilon, which predisposed it to subsequent activation by lipid cofactors. Indeed, partial proteolysis of PKCepsilon indicated that early activation of PI 3-kinase led to a conformation change in PKCepsilon that persisted as the activity of PKCepsilon cycled. We propose a two-step hypothesis for the activation of PKCepsilon in vivo. One step is stable and depends on PI 3-kinase, whereas the other is transient and may depend on the availability of lipid cofactors. Finally, these studies reveal that PI 3-kinase and PKCepsilon are capable of communicating over a relatively long time interval and begin to elucidate the mechanism.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11513725-10339426,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11513725-10712903,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11513725-10744767,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11513725-1411571,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11513725-1653029,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11513725-1846866,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11513725-7583639,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11513725-7682895,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11513725-7737456,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11513725-7798235,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11513725-8035821,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11513725-8090789,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11513725-8356071,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11513725-8380153,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11513725-8552594,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11513725-8622663,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11513725-8631300,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11513725-9601053,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11513725-9748550,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11513725-9792904,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11513725-9889098
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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 |
Sep
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
358
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
281-5
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:11513725-Cell Line,
pubmed-meshheading:11513725-Enzyme Activation,
pubmed-meshheading:11513725-Enzyme Stability,
pubmed-meshheading:11513725-Humans,
pubmed-meshheading:11513725-Isoenzymes,
pubmed-meshheading:11513725-Kinetics,
pubmed-meshheading:11513725-Models, Biological,
pubmed-meshheading:11513725-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:11513725-Phosphorylation,
pubmed-meshheading:11513725-Platelet-Derived Growth Factor,
pubmed-meshheading:11513725-Protein Conformation,
pubmed-meshheading:11513725-Protein Kinase C,
pubmed-meshheading:11513725-Protein Kinase C-epsilon,
pubmed-meshheading:11513725-Signal Transduction
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pubmed:year |
2001
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pubmed:articleTitle |
Early phosphoinositide 3-kinase activity is required for late activation of protein kinase Cepsilon in platelet-derived-growth-factor-stimulated cells: evidence for signalling across a large temporal gap.
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pubmed:affiliation |
Institute of Biotechnology, Graiciuno 8, 2028 Vilnius, Lithuania.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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