The PIDDosome, a Protein Complex Implicated in Activation of Caspase-2 in Response to Genotoxic Stress
Apoptosis is triggered by activation of initiator caspases upon complex-mediated clustering of the inactive zymogen, as occurs in the caspase-9-activating apoptosome complex. Likewise, caspase-2, which is involved in stress-induced apoptosis, is recruited into a large protein complex, the molecular...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2004-05, Vol.304 (5672), p.843-846 |
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| creator | Tinel, Antoine Tschopp, Jürg |
| description | Apoptosis is triggered by activation of initiator caspases upon complex-mediated clustering of the inactive zymogen, as occurs in the caspase-9-activating apoptosome complex. Likewise, caspase-2, which is involved in stress-induced apoptosis, is recruited into a large protein complex, the molecular composition of which remains elusive. We show that activation of caspase-2 occurs in a complex that contains the death domain-containing protein PIDD, whose expression is induced by p53, and the adaptor protein RAIDD. Increased PIDD expression resulted in spontaneous activation of caspase-2 and sensitization to apoptosis by genotoxic stimuli. Because PIDD functions in p53-mediated apoptosis, the complex assembled by PIDD and caspase-2 is likely to regulate apoptosis induced by genotoxins. |
| doi_str_mv | 10.1126/science.1095432 |
| format | Article |
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Likewise, caspase-2, which is involved in stress-induced apoptosis, is recruited into a large protein complex, the molecular composition of which remains elusive. We show that activation of caspase-2 occurs in a complex that contains the death domain-containing protein PIDD, whose expression is induced by p53, and the adaptor protein RAIDD. Increased PIDD expression resulted in spontaneous activation of caspase-2 and sensitization to apoptosis by genotoxic stimuli. Because PIDD functions in p53-mediated apoptosis, the complex assembled by PIDD and caspase-2 is likely to regulate apoptosis induced by genotoxins.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1095432</identifier><identifier>PMID: 15073321</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Association for the Advancement of Science</publisher><subject>Adaptor Proteins, Signal Transducing ; Ageing, cell death ; Antibodies ; Apoptosis ; B lymphocytes ; Biochemistry ; Biological and medical sciences ; Carrier Proteins - chemistry ; Carrier Proteins - metabolism ; Caspase 2 ; Caspases - metabolism ; Cell death ; Cell extracts ; Cell Line ; Cell Line, Tumor ; Cell physiology ; Cells ; Chemical properties ; Cloning, Molecular ; CRADD Signaling Adaptor Protein ; Death Domain Receptor Signaling Adaptor Proteins ; DNA Damage ; Doxorubicin - pharmacology ; Enzyme Activation ; Enzymes ; Etoposide - pharmacology ; Fractions ; Fundamental and applied biological sciences. Psychology ; Genetic aspects ; HeLa cells ; Humans ; Molecular and cellular biology ; Molecular biology ; Properties ; Protein Structure, Tertiary ; Proteins ; Proteins - chemistry ; Proteins - metabolism ; RNA, Small Interfering ; Scientific Concepts ; Signal Transduction ; Small interfering RNA ; T lymphocytes ; Transfection ; Tumor Suppressor Protein p53 - metabolism</subject><ispartof>Science (American Association for the Advancement of Science), 2004-05, Vol.304 (5672), p.843-846</ispartof><rights>Copyright 2004 American Association for the Advancement of Science</rights><rights>2004 INIST-CNRS</rights><rights>COPYRIGHT 2004 American Association for the Advancement of Science</rights><rights>COPYRIGHT 2004 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science May 7, 2004</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c827t-d91eca08680526e63ab511483632195aa96a4ed0b1c2f2b7e202b2d130e0604b3</citedby><cites>FETCH-LOGICAL-c827t-d91eca08680526e63ab511483632195aa96a4ed0b1c2f2b7e202b2d130e0604b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3836918$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3836918$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,2884,2885,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15753495$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15073321$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tinel, Antoine</creatorcontrib><creatorcontrib>Tschopp, Jürg</creatorcontrib><title>The PIDDosome, a Protein Complex Implicated in Activation of Caspase-2 in Response to Genotoxic Stress</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Apoptosis is triggered by activation of initiator caspases upon complex-mediated clustering of the inactive zymogen, as occurs in the caspase-9-activating apoptosome complex. Likewise, caspase-2, which is involved in stress-induced apoptosis, is recruited into a large protein complex, the molecular composition of which remains elusive. We show that activation of caspase-2 occurs in a complex that contains the death domain-containing protein PIDD, whose expression is induced by p53, and the adaptor protein RAIDD. Increased PIDD expression resulted in spontaneous activation of caspase-2 and sensitization to apoptosis by genotoxic stimuli. Because PIDD functions in p53-mediated apoptosis, the complex assembled by PIDD and caspase-2 is likely to regulate apoptosis induced by genotoxins.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Ageing, cell death</subject><subject>Antibodies</subject><subject>Apoptosis</subject><subject>B lymphocytes</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - metabolism</subject><subject>Caspase 2</subject><subject>Caspases - metabolism</subject><subject>Cell death</subject><subject>Cell extracts</subject><subject>Cell Line</subject><subject>Cell Line, Tumor</subject><subject>Cell physiology</subject><subject>Cells</subject><subject>Chemical properties</subject><subject>Cloning, Molecular</subject><subject>CRADD Signaling Adaptor Protein</subject><subject>Death Domain Receptor Signaling Adaptor Proteins</subject><subject>DNA Damage</subject><subject>Doxorubicin - pharmacology</subject><subject>Enzyme Activation</subject><subject>Enzymes</subject><subject>Etoposide - pharmacology</subject><subject>Fractions</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>Genetic aspects</topic><topic>HeLa cells</topic><topic>Humans</topic><topic>Molecular and cellular biology</topic><topic>Molecular biology</topic><topic>Properties</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins</topic><topic>Proteins - chemistry</topic><topic>Proteins - metabolism</topic><topic>RNA, Small Interfering</topic><topic>Scientific Concepts</topic><topic>Signal Transduction</topic><topic>Small interfering RNA</topic><topic>T lymphocytes</topic><topic>Transfection</topic><topic>Tumor Suppressor Protein p53 - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tinel, Antoine</creatorcontrib><creatorcontrib>Tschopp, Jürg</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE 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Likewise, caspase-2, which is involved in stress-induced apoptosis, is recruited into a large protein complex, the molecular composition of which remains elusive. We show that activation of caspase-2 occurs in a complex that contains the death domain-containing protein PIDD, whose expression is induced by p53, and the adaptor protein RAIDD. Increased PIDD expression resulted in spontaneous activation of caspase-2 and sensitization to apoptosis by genotoxic stimuli. Because PIDD functions in p53-mediated apoptosis, the complex assembled by PIDD and caspase-2 is likely to regulate apoptosis induced by genotoxins.</abstract><cop>Washington, DC</cop><pub>American Association for the Advancement of Science</pub><pmid>15073321</pmid><doi>10.1126/science.1095432</doi><tpages>4</tpages></addata></record> |
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| ispartof | Science (American Association for the Advancement of Science), 2004-05, Vol.304 (5672), p.843-846 |
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| language | eng |
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| source | MEDLINE; JSTOR Archive Collection A-Z Listing; American Association for the Advancement of Science |
| subjects | Adaptor Proteins, Signal Transducing Ageing, cell death Antibodies Apoptosis B lymphocytes Biochemistry Biological and medical sciences Carrier Proteins - chemistry Carrier Proteins - metabolism Caspase 2 Caspases - metabolism Cell death Cell extracts Cell Line Cell Line, Tumor Cell physiology Cells Chemical properties Cloning, Molecular CRADD Signaling Adaptor Protein Death Domain Receptor Signaling Adaptor Proteins DNA Damage Doxorubicin - pharmacology Enzyme Activation Enzymes Etoposide - pharmacology Fractions Fundamental and applied biological sciences. Psychology Genetic aspects HeLa cells Humans Molecular and cellular biology Molecular biology Properties Protein Structure, Tertiary Proteins Proteins - chemistry Proteins - metabolism RNA, Small Interfering Scientific Concepts Signal Transduction Small interfering RNA T lymphocytes Transfection Tumor Suppressor Protein p53 - metabolism |
| title | The PIDDosome, a Protein Complex Implicated in Activation of Caspase-2 in Response to Genotoxic Stress |
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