Regulation of Apoptosis by the p8/Prothymosin α Complex
p8 is a small-stress protein involved in several cellular functions including apoptosis. To identify its putative partners, we screened a HeLa cDNA library by using the two-hybrid technique and found that p8 binds the antiapoptotic protein prothymosin α (ProTα). Fluorescence spectroscopy, circular d...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2006-02, Vol.103 (8), p.2671-2676 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Malicet, Cédric Giroux, Valentin Vasseur, Sophie Dagorn, Jean Charles Neira, José Luis Iovanna, Juan L. |
| description | p8 is a small-stress protein involved in several cellular functions including apoptosis. To identify its putative partners, we screened a HeLa cDNA library by using the two-hybrid technique and found that p8 binds the antiapoptotic protein prothymosin α (ProTα). Fluorescence spectroscopy, circular dichroism, and NMR spectroscopy showed that p8 and ProTα formed a complex. Binding resulted in important changes in the secondary and tertiary structures of the proteins. Because p8 and ProTα form a complex, they could act in concert to regulate the apoptotic cascade. We induced apoptosis in HeLa cells by staurosporine treatment and monitored the effects of knocking down p8 and/or ProTα or overexpressing p8 and/or ProTa on caspase 3/7 and 9 activities and on cell death. Transfecting ProTα or p8 small interfering RNAs increased the activities of both caspases and the number of apoptotic nuclei. However, transfecting both small interfering RNAs resulted in no further increase. Overexpressing p8 or ProTα did not alter caspase activities, whereas overexpressing both resulted in a significant reduction of caspase activities. These results strongly suggest that the antiapoptotic response of HeLa cells upon staurosporine treatment requires expression of both p8 and ProTα. |
| doi_str_mv | 10.1073/pnas.0508955103 |
| format | Article |
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To identify its putative partners, we screened a HeLa cDNA library by using the two-hybrid technique and found that p8 binds the antiapoptotic protein prothymosin α (ProTα). Fluorescence spectroscopy, circular dichroism, and NMR spectroscopy showed that p8 and ProTα formed a complex. Binding resulted in important changes in the secondary and tertiary structures of the proteins. Because p8 and ProTα form a complex, they could act in concert to regulate the apoptotic cascade. We induced apoptosis in HeLa cells by staurosporine treatment and monitored the effects of knocking down p8 and/or ProTα or overexpressing p8 and/or ProTa on caspase 3/7 and 9 activities and on cell death. Transfecting ProTα or p8 small interfering RNAs increased the activities of both caspases and the number of apoptotic nuclei. However, transfecting both small interfering RNAs resulted in no further increase. Overexpressing p8 or ProTα did not alter caspase activities, whereas overexpressing both resulted in a significant reduction of caspase activities. These results strongly suggest that the antiapoptotic response of HeLa cells upon staurosporine treatment requires expression of both p8 and ProTα.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0508955103</identifier><identifier>PMID: 16478804</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Antibodies ; Apoptosis ; Apoptosis - genetics ; Basic Helix-Loop-Helix Transcription Factors - antagonists & inhibitors ; Basic Helix-Loop-Helix Transcription Factors - genetics ; Basic Helix-Loop-Helix Transcription Factors - metabolism ; Biological Sciences ; Caspases - metabolism ; Cell lines ; Cells ; Cellular biology ; Fluorescence ; Gene expression ; Gene Library ; HeLa Cells ; Humans ; Line spectra ; Neoplasm Proteins - antagonists & inhibitors ; Neoplasm Proteins - genetics ; Neoplasm Proteins - metabolism ; Plasmids ; Protein Precursors - antagonists & inhibitors ; Protein Precursors - genetics ; Protein Precursors - metabolism ; Proteins ; Protons ; Ribonucleic acid ; RNA ; RNA Interference ; RNA, Small Interfering - genetics ; RNA, Small Interfering - physiology ; Small interfering RNA ; Spectrum Analysis ; Staurosporine - pharmacology ; Thymosin - analogs & derivatives ; Thymosin - antagonists & inhibitors ; Thymosin - genetics ; Thymosin - metabolism ; Two-Hybrid System Techniques</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2006-02, Vol.103 (8), p.2671-2676</ispartof><rights>Copyright 2006 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Feb 21, 2006</rights><rights>2006 by The National Academy of Sciences of the USA 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c526t-4736c4c4d4c4cc5141857174b57fc89044b2e43f381867f8b189146ba09915983</citedby><cites>FETCH-LOGICAL-c526t-4736c4c4d4c4cc5141857174b57fc89044b2e43f381867f8b189146ba09915983</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/103/8.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/30049471$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/30049471$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,315,729,782,786,805,887,27931,27932,53798,53800,58024,58257</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16478804$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Malicet, Cédric</creatorcontrib><creatorcontrib>Giroux, Valentin</creatorcontrib><creatorcontrib>Vasseur, Sophie</creatorcontrib><creatorcontrib>Dagorn, Jean Charles</creatorcontrib><creatorcontrib>Neira, José Luis</creatorcontrib><creatorcontrib>Iovanna, Juan L.</creatorcontrib><title>Regulation of Apoptosis by the p8/Prothymosin α Complex</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>p8 is a small-stress protein involved in several cellular functions including apoptosis. To identify its putative partners, we screened a HeLa cDNA library by using the two-hybrid technique and found that p8 binds the antiapoptotic protein prothymosin α (ProTα). Fluorescence spectroscopy, circular dichroism, and NMR spectroscopy showed that p8 and ProTα formed a complex. Binding resulted in important changes in the secondary and tertiary structures of the proteins. Because p8 and ProTα form a complex, they could act in concert to regulate the apoptotic cascade. We induced apoptosis in HeLa cells by staurosporine treatment and monitored the effects of knocking down p8 and/or ProTα or overexpressing p8 and/or ProTa on caspase 3/7 and 9 activities and on cell death. Transfecting ProTα or p8 small interfering RNAs increased the activities of both caspases and the number of apoptotic nuclei. However, transfecting both small interfering RNAs resulted in no further increase. Overexpressing p8 or ProTα did not alter caspase activities, whereas overexpressing both resulted in a significant reduction of caspase activities. These results strongly suggest that the antiapoptotic response of HeLa cells upon staurosporine treatment requires expression of both p8 and ProTα.</description><subject>Antibodies</subject><subject>Apoptosis</subject><subject>Apoptosis - genetics</subject><subject>Basic Helix-Loop-Helix Transcription Factors - antagonists & inhibitors</subject><subject>Basic Helix-Loop-Helix Transcription Factors - genetics</subject><subject>Basic Helix-Loop-Helix Transcription Factors - metabolism</subject><subject>Biological Sciences</subject><subject>Caspases - metabolism</subject><subject>Cell lines</subject><subject>Cells</subject><subject>Cellular biology</subject><subject>Fluorescence</subject><subject>Gene expression</subject><subject>Gene Library</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Line spectra</subject><subject>Neoplasm Proteins - antagonists & inhibitors</subject><subject>Neoplasm Proteins - genetics</subject><subject>Neoplasm Proteins - metabolism</subject><subject>Plasmids</subject><subject>Protein Precursors - antagonists & inhibitors</subject><subject>Protein Precursors - genetics</subject><subject>Protein Precursors - metabolism</subject><subject>Proteins</subject><subject>Protons</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>RNA Interference</subject><subject>RNA, Small Interfering - genetics</subject><subject>RNA, Small Interfering - physiology</subject><subject>Small interfering RNA</subject><subject>Spectrum Analysis</subject><subject>Staurosporine - pharmacology</subject><subject>Thymosin - analogs & derivatives</subject><subject>Thymosin - antagonists & inhibitors</subject><subject>Thymosin - genetics</subject><subject>Thymosin - metabolism</subject><subject>Two-Hybrid System Techniques</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1q3DAURkVoaKbTrrtqMV20K2eurP9NIAxNGggklHYtbEXOeLAtV5JL5rHyInmmysyQSbJoFkIgnXt0rz6EPmI4xiDIYujLcAwMpGIMAzlAMwwK55wqeINmAIXIJS3oEXoXwhoAFJPwFh1hToWUQGdI_rS3Y1vGxvWZq7PTwQ3RhSZk1SaLK5sNcnHtXVxtunTaZw_32dJ1Q2vv3qPDumyD_bDb5-j32fdfyx_55dX5xfL0Mjes4DGngnBDDb1JyxiGKZZMYEErJmojFVBaFZaSmkgsuahlhaXClFclKIWZkmSOTrbeYaw6e2NsH33Z6sE3Xek32pWNfn7TNyt96_7q9BQRkifB153Auz-jDVF3TTC2bcveujFoLlTBC45fBbEAmaQT-OUFuHaj79Mv6AJwmgRSFHO02ELGuxC8rR9bxqCn7PSUnd5nlyo-P510z-_CegJMlXsd0VIXXEyNffsvoOuxbaO9i4n8tCXXITr_iBIAqmgy_QN82LT-</recordid><startdate>20060221</startdate><enddate>20060221</enddate><creator>Malicet, Cédric</creator><creator>Giroux, Valentin</creator><creator>Vasseur, Sophie</creator><creator>Dagorn, Jean Charles</creator><creator>Neira, José Luis</creator><creator>Iovanna, Juan L.</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20060221</creationdate><title>Regulation of Apoptosis by the p8/Prothymosin α Complex</title><author>Malicet, Cédric ; 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To identify its putative partners, we screened a HeLa cDNA library by using the two-hybrid technique and found that p8 binds the antiapoptotic protein prothymosin α (ProTα). Fluorescence spectroscopy, circular dichroism, and NMR spectroscopy showed that p8 and ProTα formed a complex. Binding resulted in important changes in the secondary and tertiary structures of the proteins. Because p8 and ProTα form a complex, they could act in concert to regulate the apoptotic cascade. We induced apoptosis in HeLa cells by staurosporine treatment and monitored the effects of knocking down p8 and/or ProTα or overexpressing p8 and/or ProTa on caspase 3/7 and 9 activities and on cell death. Transfecting ProTα or p8 small interfering RNAs increased the activities of both caspases and the number of apoptotic nuclei. However, transfecting both small interfering RNAs resulted in no further increase. Overexpressing p8 or ProTα did not alter caspase activities, whereas overexpressing both resulted in a significant reduction of caspase activities. These results strongly suggest that the antiapoptotic response of HeLa cells upon staurosporine treatment requires expression of both p8 and ProTα.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>16478804</pmid><doi>10.1073/pnas.0508955103</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Antibodies Apoptosis Apoptosis - genetics Basic Helix-Loop-Helix Transcription Factors - antagonists & inhibitors Basic Helix-Loop-Helix Transcription Factors - genetics Basic Helix-Loop-Helix Transcription Factors - metabolism Biological Sciences Caspases - metabolism Cell lines Cells Cellular biology Fluorescence Gene expression Gene Library HeLa Cells Humans Line spectra Neoplasm Proteins - antagonists & inhibitors Neoplasm Proteins - genetics Neoplasm Proteins - metabolism Plasmids Protein Precursors - antagonists & inhibitors Protein Precursors - genetics Protein Precursors - metabolism Proteins Protons Ribonucleic acid RNA RNA Interference RNA, Small Interfering - genetics RNA, Small Interfering - physiology Small interfering RNA Spectrum Analysis Staurosporine - pharmacology Thymosin - analogs & derivatives Thymosin - antagonists & inhibitors Thymosin - genetics Thymosin - metabolism Two-Hybrid System Techniques |
| title | Regulation of Apoptosis by the p8/Prothymosin α Complex |
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