Cytochrome c speeds up caspase cascade activation by blocking 14-3-3ε-dependent Apaf-1 inhibition
Apoptosis is a highly regulated form of programmed cell death, essential to the development and homeostasis of multicellular organisms. Cytochrome c is a central figure in the activation of the apoptotic intrinsic pathway, thereby activating the caspase cascade through its interaction with Apaf-1. O...
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| Veröffentlicht in: | Cell death & disease 2018-03, Vol.9 (3), p.365-12, Article 365 |
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| creator | Elena-Real, Carlos A. Díaz-Quintana, Antonio González-Arzola, Katiuska Velázquez-Campoy, Adrián Orzáez, Mar López-Rivas, Abelardo Gil-Caballero, Sergio De la Rosa, Miguel Á. Díaz-Moreno, Irene |
| description | Apoptosis is a highly regulated form of programmed cell death, essential to the development and homeostasis of multicellular organisms. Cytochrome
c
is a central figure in the activation of the apoptotic intrinsic pathway, thereby activating the caspase cascade through its interaction with Apaf-1. Our recent studies have revealed 14-3-3ε (a direct inhibitor of Apaf-1) as a cytosolic cytochrome
c
target. Here we explore the cytochrome
c
/ 14-3-3ε interaction and show the ability of cytochrome
c
to block 14-3-3ε-mediated Apaf-1 inhibition, thereby unveiling a novel function for cytochrome
c
as an indirect activator of caspase-9/3. We have used calorimetry, NMR spectroscopy, site mutagenesis and computational calculations to provide an insight into the structural features of the cytochrome
c
/ 14-3-3ε complex. Overall, these findings suggest an additional cytochrome
c
-mediated mechanism to modulate apoptosome formation, shedding light onto the rigorous apoptotic regulation network. |
| doi_str_mv | 10.1038/s41419-018-0408-1 |
| format | Article |
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c
is a central figure in the activation of the apoptotic intrinsic pathway, thereby activating the caspase cascade through its interaction with Apaf-1. Our recent studies have revealed 14-3-3ε (a direct inhibitor of Apaf-1) as a cytosolic cytochrome
c
target. Here we explore the cytochrome
c
/ 14-3-3ε interaction and show the ability of cytochrome
c
to block 14-3-3ε-mediated Apaf-1 inhibition, thereby unveiling a novel function for cytochrome
c
as an indirect activator of caspase-9/3. We have used calorimetry, NMR spectroscopy, site mutagenesis and computational calculations to provide an insight into the structural features of the cytochrome
c
/ 14-3-3ε complex. Overall, these findings suggest an additional cytochrome
c
-mediated mechanism to modulate apoptosome formation, shedding light onto the rigorous apoptotic regulation network.</description><identifier>ISSN: 2041-4889</identifier><identifier>EISSN: 2041-4889</identifier><identifier>DOI: 10.1038/s41419-018-0408-1</identifier><identifier>PMID: 29511177</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>101/6 ; 13/2 ; Antibodies ; Apaf-1 protein ; Apoptosis ; Biochemistry ; Biomedical and Life Sciences ; Calorimetry ; Caspase ; Caspase-9 ; Cell Biology ; Cell Culture ; Cell death ; Computer applications ; Cytochrome ; Cytochrome c ; Homeostasis ; Immunology ; Life Sciences ; Magnetic resonance spectroscopy ; Mitochondrial DNA ; Mutagenesis ; NMR ; Nuclear magnetic resonance</subject><ispartof>Cell death & disease, 2018-03, Vol.9 (3), p.365-12, Article 365</ispartof><rights>The Author(s) 2018</rights><rights>2018. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c400t-393266626e87bff2c2950cbc4a0faaae4b074596751d5007e1f735ad85964bb3</citedby><cites>FETCH-LOGICAL-c400t-393266626e87bff2c2950cbc4a0faaae4b074596751d5007e1f735ad85964bb3</cites><orcidid>0000-0003-1187-5737 ; 0000-0001-8973-8009</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5840378/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5840378/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,865,886,27926,27927,41122,42191,51578,53793,53795</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29511177$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Elena-Real, Carlos A.</creatorcontrib><creatorcontrib>Díaz-Quintana, Antonio</creatorcontrib><creatorcontrib>González-Arzola, Katiuska</creatorcontrib><creatorcontrib>Velázquez-Campoy, Adrián</creatorcontrib><creatorcontrib>Orzáez, Mar</creatorcontrib><creatorcontrib>López-Rivas, Abelardo</creatorcontrib><creatorcontrib>Gil-Caballero, Sergio</creatorcontrib><creatorcontrib>De la Rosa, Miguel Á.</creatorcontrib><creatorcontrib>Díaz-Moreno, Irene</creatorcontrib><title>Cytochrome c speeds up caspase cascade activation by blocking 14-3-3ε-dependent Apaf-1 inhibition</title><title>Cell death & disease</title><addtitle>Cell Death Dis</addtitle><addtitle>Cell Death Dis</addtitle><description>Apoptosis is a highly regulated form of programmed cell death, essential to the development and homeostasis of multicellular organisms. Cytochrome
c
is a central figure in the activation of the apoptotic intrinsic pathway, thereby activating the caspase cascade through its interaction with Apaf-1. Our recent studies have revealed 14-3-3ε (a direct inhibitor of Apaf-1) as a cytosolic cytochrome
c
target. Here we explore the cytochrome
c
/ 14-3-3ε interaction and show the ability of cytochrome
c
to block 14-3-3ε-mediated Apaf-1 inhibition, thereby unveiling a novel function for cytochrome
c
as an indirect activator of caspase-9/3. We have used calorimetry, NMR spectroscopy, site mutagenesis and computational calculations to provide an insight into the structural features of the cytochrome
c
/ 14-3-3ε complex. Overall, these findings suggest an additional cytochrome
c
-mediated mechanism to modulate apoptosome formation, shedding light onto the rigorous apoptotic regulation network.</description><subject>101/6</subject><subject>13/2</subject><subject>Antibodies</subject><subject>Apaf-1 protein</subject><subject>Apoptosis</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Calorimetry</subject><subject>Caspase</subject><subject>Caspase-9</subject><subject>Cell Biology</subject><subject>Cell Culture</subject><subject>Cell death</subject><subject>Computer applications</subject><subject>Cytochrome</subject><subject>Cytochrome c</subject><subject>Homeostasis</subject><subject>Immunology</subject><subject>Life Sciences</subject><subject>Magnetic resonance spectroscopy</subject><subject>Mitochondrial DNA</subject><subject>Mutagenesis</subject><subject>NMR</subject><subject>Nuclear magnetic resonance</subject><issn>2041-4889</issn><issn>2041-4889</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kc1q3DAUhU1pSUKaB8imCLrpRq2ufix5UwhD-gOBbrIXkizPKPVIrmQH5sH6Gn2myEyapoVqc4Xud4_O5TTNJZD3QJj6UDhw6DABhQknCsOL5owSDpgr1b18dj9tLkq5I_UwRqhoT5pT2gkAkPKssZvDnNwup71HDpXJ-76gZULOlMkUv1Zneo-Mm8O9mUOKyB6QHZP7HuIWAccMs18_ce8nH3sfZ3Q1mQEDCnEXbFgHXjevBjMWf_FYz5vbT9e3my_45tvnr5urG-w4ITNmHaNt29LWK2mHgbpqkjjruCGDMcZzSyQXXSsF9IIQ6WGQTJhe1TduLTtvPh5lp8Xufe-ql2xGPeWwN_mgkwn6704MO71N91ooTphUVeDdo0BOPxZfZr0PxflxNNGnpWhKAFpgXMiKvv0HvUtLjnW7leq4UFStgnCkXE6lZD88mQGi1wz1MUNdM9RrhhrqzJvnWzxN_E6sAvQIlNqKW5__fP1_1Qchf6bM</recordid><startdate>20180306</startdate><enddate>20180306</enddate><creator>Elena-Real, Carlos A.</creator><creator>Díaz-Quintana, Antonio</creator><creator>González-Arzola, Katiuska</creator><creator>Velázquez-Campoy, Adrián</creator><creator>Orzáez, Mar</creator><creator>López-Rivas, Abelardo</creator><creator>Gil-Caballero, Sergio</creator><creator>De la Rosa, Miguel Á.</creator><creator>Díaz-Moreno, Irene</creator><general>Nature Publishing Group UK</general><general>Springer Nature B.V</general><scope>C6C</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-1187-5737</orcidid><orcidid>https://orcid.org/0000-0001-8973-8009</orcidid></search><sort><creationdate>20180306</creationdate><title>Cytochrome c speeds up caspase cascade activation by blocking 14-3-3ε-dependent Apaf-1 inhibition</title><author>Elena-Real, Carlos A. ; Díaz-Quintana, Antonio ; González-Arzola, Katiuska ; Velázquez-Campoy, Adrián ; Orzáez, Mar ; López-Rivas, Abelardo ; Gil-Caballero, Sergio ; De la Rosa, Miguel Á. ; Díaz-Moreno, Irene</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c400t-393266626e87bff2c2950cbc4a0faaae4b074596751d5007e1f735ad85964bb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>101/6</topic><topic>13/2</topic><topic>Antibodies</topic><topic>Apaf-1 protein</topic><topic>Apoptosis</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Calorimetry</topic><topic>Caspase</topic><topic>Caspase-9</topic><topic>Cell Biology</topic><topic>Cell Culture</topic><topic>Cell death</topic><topic>Computer applications</topic><topic>Cytochrome</topic><topic>Cytochrome c</topic><topic>Homeostasis</topic><topic>Immunology</topic><topic>Life Sciences</topic><topic>Magnetic resonance spectroscopy</topic><topic>Mitochondrial DNA</topic><topic>Mutagenesis</topic><topic>NMR</topic><topic>Nuclear magnetic resonance</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Elena-Real, Carlos A.</creatorcontrib><creatorcontrib>Díaz-Quintana, Antonio</creatorcontrib><creatorcontrib>González-Arzola, Katiuska</creatorcontrib><creatorcontrib>Velázquez-Campoy, Adrián</creatorcontrib><creatorcontrib>Orzáez, Mar</creatorcontrib><creatorcontrib>López-Rivas, Abelardo</creatorcontrib><creatorcontrib>Gil-Caballero, Sergio</creatorcontrib><creatorcontrib>De la Rosa, Miguel Á.</creatorcontrib><creatorcontrib>Díaz-Moreno, Irene</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell death & disease</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Elena-Real, Carlos A.</au><au>Díaz-Quintana, Antonio</au><au>González-Arzola, Katiuska</au><au>Velázquez-Campoy, Adrián</au><au>Orzáez, Mar</au><au>López-Rivas, Abelardo</au><au>Gil-Caballero, Sergio</au><au>De la Rosa, Miguel Á.</au><au>Díaz-Moreno, Irene</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cytochrome c speeds up caspase cascade activation by blocking 14-3-3ε-dependent Apaf-1 inhibition</atitle><jtitle>Cell death & disease</jtitle><stitle>Cell Death Dis</stitle><addtitle>Cell Death Dis</addtitle><date>2018-03-06</date><risdate>2018</risdate><volume>9</volume><issue>3</issue><spage>365</spage><epage>12</epage><pages>365-12</pages><artnum>365</artnum><issn>2041-4889</issn><eissn>2041-4889</eissn><abstract>Apoptosis is a highly regulated form of programmed cell death, essential to the development and homeostasis of multicellular organisms. Cytochrome
c
is a central figure in the activation of the apoptotic intrinsic pathway, thereby activating the caspase cascade through its interaction with Apaf-1. Our recent studies have revealed 14-3-3ε (a direct inhibitor of Apaf-1) as a cytosolic cytochrome
c
target. Here we explore the cytochrome
c
/ 14-3-3ε interaction and show the ability of cytochrome
c
to block 14-3-3ε-mediated Apaf-1 inhibition, thereby unveiling a novel function for cytochrome
c
as an indirect activator of caspase-9/3. We have used calorimetry, NMR spectroscopy, site mutagenesis and computational calculations to provide an insight into the structural features of the cytochrome
c
/ 14-3-3ε complex. Overall, these findings suggest an additional cytochrome
c
-mediated mechanism to modulate apoptosome formation, shedding light onto the rigorous apoptotic regulation network.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>29511177</pmid><doi>10.1038/s41419-018-0408-1</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0003-1187-5737</orcidid><orcidid>https://orcid.org/0000-0001-8973-8009</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | 101/6 13/2 Antibodies Apaf-1 protein Apoptosis Biochemistry Biomedical and Life Sciences Calorimetry Caspase Caspase-9 Cell Biology Cell Culture Cell death Computer applications Cytochrome Cytochrome c Homeostasis Immunology Life Sciences Magnetic resonance spectroscopy Mitochondrial DNA Mutagenesis NMR Nuclear magnetic resonance |
| title | Cytochrome c speeds up caspase cascade activation by blocking 14-3-3ε-dependent Apaf-1 inhibition |
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