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Several nuclear events during apoptosis depend on caspase-3 activation but do not constitute a common pathway
A number of nuclear events occur during apoptosis, including DNA laddering, nuclear lamina breakdown, phosphorylation of histones H2B and histone H2AX, and the tight binding to chromatin of HMGB1 and CAD, the nuclease responsible for DNA laddering. We have performed an epistasis analysis to investig...
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Published in: | PloS one 2009-07, Vol.4 (7), p.e6234-e6234 |
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description | A number of nuclear events occur during apoptosis, including DNA laddering, nuclear lamina breakdown, phosphorylation of histones H2B and histone H2AX, and the tight binding to chromatin of HMGB1 and CAD, the nuclease responsible for DNA laddering. We have performed an epistasis analysis to investigate whether these events cluster together in pathways. We find that all depend directly or indirectly on caspase-3 activation. CAD activation, H2AX phosphorylation and DNA laddering cluster together into a pathway, but all other events appear to be independent of each other downstream of caspase-3, and likely evolved subject to different functional pressures. |
doi_str_mv | 10.1371/journal.pone.0006234 |
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We have performed an epistasis analysis to investigate whether these events cluster together in pathways. We find that all depend directly or indirectly on caspase-3 activation. CAD activation, H2AX phosphorylation and DNA laddering cluster together into a pathway, but all other events appear to be independent of each other downstream of caspase-3, and likely evolved subject to different functional pressures.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0006234</identifier><identifier>PMID: 19641621</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Activation ; Apoptosis ; Base Sequence ; Biochemistry ; Breast cancer ; Caspase ; Caspase 3 - metabolism ; Caspase 6 - metabolism ; Caspase-3 ; Cell Biology/Cellular Death and Stress Responses ; Cell Line ; Cell Nucleus - enzymology ; Chromatin ; Chromatin - metabolism ; Clusters ; Cytokines ; Deoxyribonucleic acid ; DNA ; DNA binding proteins ; DNA damage ; DNA fragmentation ; DNA Primers ; Enzyme Activation ; Epistasis ; Fluorescence ; Genetic research ; Histone H2A ; Histones ; Histones - metabolism ; HMGB1 protein ; HMGB1 Protein - metabolism ; Humans ; Microscopy ; Molecular Biology/Chromatin Structure ; Morphology ; Nuclease ; Nucleoproteins ; Pathogenesis ; Phosphorylation ; Proteins ; Recovery (Medical) ; Rodents</subject><ispartof>PloS one, 2009-07, Vol.4 (7), p.e6234-e6234</ispartof><rights>COPYRIGHT 2009 Public Library of Science</rights><rights>2009 Trisciuoglio, Bianchi. This is an open-access article distributed under the terms of the Creative Commons Attribution License (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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We have performed an epistasis analysis to investigate whether these events cluster together in pathways. We find that all depend directly or indirectly on caspase-3 activation. CAD activation, H2AX phosphorylation and DNA laddering cluster together into a pathway, but all other events appear to be independent of each other downstream of caspase-3, and likely evolved subject to different functional pressures.</description><subject>Activation</subject><subject>Apoptosis</subject><subject>Base Sequence</subject><subject>Biochemistry</subject><subject>Breast cancer</subject><subject>Caspase</subject><subject>Caspase 3 - metabolism</subject><subject>Caspase 6 - metabolism</subject><subject>Caspase-3</subject><subject>Cell Biology/Cellular Death and Stress Responses</subject><subject>Cell Line</subject><subject>Cell Nucleus - enzymology</subject><subject>Chromatin</subject><subject>Chromatin - metabolism</subject><subject>Clusters</subject><subject>Cytokines</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA binding proteins</subject><subject>DNA damage</subject><subject>DNA fragmentation</subject><subject>DNA Primers</subject><subject>Enzyme Activation</subject><subject>Epistasis</subject><subject>Fluorescence</subject><subject>Genetic research</subject><subject>Histone H2A</subject><subject>Histones</subject><subject>Histones - metabolism</subject><subject>HMGB1 protein</subject><subject>HMGB1 Protein - metabolism</subject><subject>Humans</subject><subject>Microscopy</subject><subject>Molecular Biology/Chromatin Structure</subject><subject>Morphology</subject><subject>Nuclease</subject><subject>Nucleoproteins</subject><subject>Pathogenesis</subject><subject>Phosphorylation</subject><subject>Proteins</subject><subject>Recovery (Medical)</subject><subject>Rodents</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNqNkl2L1DAUhoso7jr6D0QDwoIXHfPRpu3NwrL4MbCw4Kq34TQ9ncnQJrVJR_ffm3GqzogXkosmJ885p-fNmyTPGV0yUbA3WzeNFrrl4CwuKaWSi-xBcs4qwVPJqXh4tD9Lnni_pTQXpZSPkzNWyYxJzs6T_g53OEJH7KQ7hJHEow2eNNNo7JrA4IbgvIkBHNA2xFmiwQ_gMRUEdDA7CCYG6ymQxhHrAtHO-mDCFJBAPPR9vB4gbL7B_dPkUQudx2fzd5F8fvf20_WH9Ob2_er66ibVUvKQQllnQlesaDNWlqIEqKHJalE1bV0JoBSozJFTLCXSIs9F3XIUKCnWbSkiskheHuoOnfNqVsorxitGcykrHonVgWgcbNUwmh7Ge-XAqJ8BN64VjMFETRTLG6SCaSFEm1WUlpBraIuyrcuKSbrvdjl3m-oeGx0FjIqeFD29sWaj1m6neMFEFp9nkVzMBUb3dUIfVG-8xq4Di27ySha5yGTOIvjqL_Dfsy0P1Bri7xvbuthVx9Vgb-LrYGti_CoreCXiAHlMeH2SEJmA38MaJu_V6u7j_7O3X07ZiyN2g9CFjXfdtHeMPwWzA6hH5_2I7W_xGFV7t_-aU-3drma3x7QXx8L_SZrtLX4ApHz8Bw</recordid><startdate>20090729</startdate><enddate>20090729</enddate><creator>Trisciuoglio, Lisa</creator><creator>Bianchi, Marco Emilio</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20090729</creationdate><title>Several nuclear events during apoptosis depend on caspase-3 activation but do not constitute a common pathway</title><author>Trisciuoglio, Lisa ; Bianchi, Marco Emilio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c662t-a8b43c917f418838aabad4b39dfb93a00a065e20e86e07553bf2e3e60ebf83b93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Activation</topic><topic>Apoptosis</topic><topic>Base Sequence</topic><topic>Biochemistry</topic><topic>Breast cancer</topic><topic>Caspase</topic><topic>Caspase 3 - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Trisciuoglio, Lisa</au><au>Bianchi, Marco Emilio</au><au>Goldman, Gustavo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Several nuclear events during apoptosis depend on caspase-3 activation but do not constitute a common pathway</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2009-07-29</date><risdate>2009</risdate><volume>4</volume><issue>7</issue><spage>e6234</spage><epage>e6234</epage><pages>e6234-e6234</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>A number of nuclear events occur during apoptosis, including DNA laddering, nuclear lamina breakdown, phosphorylation of histones H2B and histone H2AX, and the tight binding to chromatin of HMGB1 and CAD, the nuclease responsible for DNA laddering. We have performed an epistasis analysis to investigate whether these events cluster together in pathways. We find that all depend directly or indirectly on caspase-3 activation. CAD activation, H2AX phosphorylation and DNA laddering cluster together into a pathway, but all other events appear to be independent of each other downstream of caspase-3, and likely evolved subject to different functional pressures.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>19641621</pmid><doi>10.1371/journal.pone.0006234</doi><tpages>e6234</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Activation Apoptosis Base Sequence Biochemistry Breast cancer Caspase Caspase 3 - metabolism Caspase 6 - metabolism Caspase-3 Cell Biology/Cellular Death and Stress Responses Cell Line Cell Nucleus - enzymology Chromatin Chromatin - metabolism Clusters Cytokines Deoxyribonucleic acid DNA DNA binding proteins DNA damage DNA fragmentation DNA Primers Enzyme Activation Epistasis Fluorescence Genetic research Histone H2A Histones Histones - metabolism HMGB1 protein HMGB1 Protein - metabolism Humans Microscopy Molecular Biology/Chromatin Structure Morphology Nuclease Nucleoproteins Pathogenesis Phosphorylation Proteins Recovery (Medical) Rodents |
title | Several nuclear events during apoptosis depend on caspase-3 activation but do not constitute a common pathway |
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