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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5318
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pubmed:dateCreated |
1997-6-17
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pubmed:abstractText |
Apoptosis of Jurkat T cells induced the caspase-mediated proteolytic cleavage of p21-activated kinase 2 (PAK2). Cleavage occurred between the amino-terminal regulatory domain and the carboxyl-terminal catalytic domain, which generated a constitutively active PAK2 fragment. Stable Jurkat cell lines that expressed a dominant-negative PAK mutant were resistant to the Fas-induced formation of apoptotic bodies, but had an enhanced externalization of phosphatidylserine at the cell surface. Thus, proteolytic activation of PAK2 represents a guanosine triphosphatase-independent mechanism of PAK regulation that allows PAK2 to regulate morphological changes that are seen in apoptotic cells.
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pubmed:grant |
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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/Amino Acid Chloromethyl Ketones,
http://linkedlifedata.com/resource/pubmed/chemical/CASP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Proteinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/FASLG protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Fas Ligand Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/N-acetyl-tyrosyl-valyl-alanyl-aspart...,
http://linkedlifedata.com/resource/pubmed/chemical/PAK2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylserines,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/p21-Activated Kinases
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1571-4
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:9171063-Amino Acid Chloromethyl Ketones,
pubmed-meshheading:9171063-Apoptosis,
pubmed-meshheading:9171063-Binding Sites,
pubmed-meshheading:9171063-Caspase 3,
pubmed-meshheading:9171063-Caspases,
pubmed-meshheading:9171063-Cell Membrane,
pubmed-meshheading:9171063-Cysteine Endopeptidases,
pubmed-meshheading:9171063-Cysteine Proteinase Inhibitors,
pubmed-meshheading:9171063-Enzyme Activation,
pubmed-meshheading:9171063-Fas Ligand Protein,
pubmed-meshheading:9171063-Humans,
pubmed-meshheading:9171063-Jurkat Cells,
pubmed-meshheading:9171063-Membrane Glycoproteins,
pubmed-meshheading:9171063-Phosphatidylserines,
pubmed-meshheading:9171063-Protein-Serine-Threonine Kinases,
pubmed-meshheading:9171063-Recombinant Proteins,
pubmed-meshheading:9171063-T-Lymphocytes,
pubmed-meshheading:9171063-p21-Activated Kinases
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pubmed:year |
1997
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pubmed:articleTitle |
Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2.
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pubmed:affiliation |
Department of Immunology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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