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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 |
2007-6-1
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pubmed:abstractText |
Ras activation as a consequence of antigen receptor (T-cell receptor; TCR) engagement on T lymphocytes is required for T-cell development, selection and function. Lymphocyte function-associated antigen-1 (LFA-1) mediates lymphocyte adhesion, stabilization of the immune synapse and bidirectional signalling. Using a fluorescent biosensor we found that TCR activation with or without costimulation of CD28 led to activation of Ras only on the Golgi apparatus, whereas costimulation with LFA-1 induced Ras activation on both the Golgi and the plasma membrane. Ras activation on both compartments required RasGRP1, an exchange factor regulated by calcium and diacylglycerol (DAG), but phospholipase C (PLC) activity was required only for activation on the Golgi. Engagement of LFA-1 increased DAG levels at the plasma membrane by stimulating phospholipase D (PLD). PLD2 and phosphatidic acid phosphatase (PAP) were required for Ras activation on the plasma membrane. Thus, LFA-1 acts through PLD2 to reshape the pattern of Ras activation downstream of the TCR.
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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/Antigens, CD28,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Diglycerides,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Lymphocyte Function-Associated...,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase D,
http://linkedlifedata.com/resource/pubmed/chemical/RASGRP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases,
http://linkedlifedata.com/resource/pubmed/chemical/phospholipase D2,
http://linkedlifedata.com/resource/pubmed/chemical/ras Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1465-7392
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
713-9
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:17486117-Animals,
pubmed-meshheading:17486117-Antigens, CD28,
pubmed-meshheading:17486117-Cell Communication,
pubmed-meshheading:17486117-Cell Membrane,
pubmed-meshheading:17486117-DNA-Binding Proteins,
pubmed-meshheading:17486117-Diglycerides,
pubmed-meshheading:17486117-Enzyme Activation,
pubmed-meshheading:17486117-Golgi Apparatus,
pubmed-meshheading:17486117-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:17486117-Humans,
pubmed-meshheading:17486117-Jurkat Cells,
pubmed-meshheading:17486117-Lymphocyte Function-Associated Antigen-1,
pubmed-meshheading:17486117-Mice,
pubmed-meshheading:17486117-Mice, Inbred C57BL,
pubmed-meshheading:17486117-Mice, Knockout,
pubmed-meshheading:17486117-Phospholipase D,
pubmed-meshheading:17486117-Receptors, Antigen, T-Cell,
pubmed-meshheading:17486117-Signal Transduction,
pubmed-meshheading:17486117-T-Lymphocytes,
pubmed-meshheading:17486117-Type C Phospholipases,
pubmed-meshheading:17486117-ras Proteins
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pubmed:year |
2007
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pubmed:articleTitle |
The lymphocyte function-associated antigen-1 receptor costimulates plasma membrane Ras via phospholipase D2.
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pubmed:affiliation |
Department of Medicine, NYU School of Medicine, New York, NY 10016, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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