rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2009-9-28
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pubmed:abstractText |
Caspase-2 is an initiator caspase activated in response to heat shock and other stressors that induce apoptosis. Activation of caspase-2 requires induced proximity resulting after recruitment to caspase-2 activation complexes such as the PIDDosome. We have adapted bimolecular fluorescence complementation (BiFC) to measure caspase-2 induced proximity in real time in single cells. Nonfluorescent fragments of the fluorescent protein Venus that can associate to reform the fluorescent complex were fused to caspase-2, allowing visualization and kinetic measurements of caspase-2 induced proximity after heat shock and other stresses. This revealed that the caspase-2 activation platform occurred in the cytosol and not in the nucleus in response to heat shock, DNA damage, cytoskeletal disruption, and other treatments. Activation, as measured by this approach, in response to heat shock was RAIDD dependent and upstream of mitochondrial outer-membrane permeabilization. Furthermore, we identify Hsp90alpha as a key negative regulator of heat shock-induced caspase-2 activation.
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pubmed:grant |
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pubmed:commentsCorrections |
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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/Apoptotic Protease-Activating...,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/CRADD Signaling Adaptor Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Cradd protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fas-Associated Death Domain Protein,
http://linkedlifedata.com/resource/pubmed/chemical/HSP90 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HSP90alpha protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Hsf1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Tubulin Modulators,
http://linkedlifedata.com/resource/pubmed/chemical/yellow fluorescent protein, Bacteria
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1097-4164
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
24
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pubmed:volume |
35
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
830-40
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pubmed:dateRevised |
2011-8-1
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pubmed:meshHeading |
pubmed-meshheading:19782032-Animals,
pubmed-meshheading:19782032-Apoptosis,
pubmed-meshheading:19782032-Apoptotic Protease-Activating Factor 1,
pubmed-meshheading:19782032-Bacterial Proteins,
pubmed-meshheading:19782032-Biosensing Techniques,
pubmed-meshheading:19782032-CRADD Signaling Adaptor Protein,
pubmed-meshheading:19782032-Caspase 2,
pubmed-meshheading:19782032-Cytoplasm,
pubmed-meshheading:19782032-DNA Damage,
pubmed-meshheading:19782032-DNA-Binding Proteins,
pubmed-meshheading:19782032-Enzyme Activation,
pubmed-meshheading:19782032-Fas-Associated Death Domain Protein,
pubmed-meshheading:19782032-HSP90 Heat-Shock Proteins,
pubmed-meshheading:19782032-HeLa Cells,
pubmed-meshheading:19782032-Hot Temperature,
pubmed-meshheading:19782032-Humans,
pubmed-meshheading:19782032-Kinetics,
pubmed-meshheading:19782032-Luminescent Proteins,
pubmed-meshheading:19782032-Mice,
pubmed-meshheading:19782032-Mice, Knockout,
pubmed-meshheading:19782032-Microscopy, Confocal,
pubmed-meshheading:19782032-Mitochondria,
pubmed-meshheading:19782032-Mutagenesis, Site-Directed,
pubmed-meshheading:19782032-Protein Multimerization,
pubmed-meshheading:19782032-RNA Interference,
pubmed-meshheading:19782032-Recombinant Fusion Proteins,
pubmed-meshheading:19782032-Signal Transduction,
pubmed-meshheading:19782032-Stress, Physiological,
pubmed-meshheading:19782032-Transcription Factors,
pubmed-meshheading:19782032-Transfection,
pubmed-meshheading:19782032-Tubulin Modulators
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pubmed:year |
2009
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pubmed:articleTitle |
Characterization of cytoplasmic caspase-2 activation by induced proximity.
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pubmed:affiliation |
Department of Immunology, St. Jude Children's Research Hospital, 262 Danny Thomas Place, Memphis, TN 38105, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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