FATE1 antagonizes calcium- and drug-induced apoptosis by uncoupling ER and mitochondria
Several stimuli induce programmed cell death by increasing Ca 2+ transfer from the endoplasmic reticulum (ER) to mitochondria. Perturbation of this process has a special relevance in pathologies as cancer and neurodegenerative disorders. Mitochondrial Ca 2+ uptake mainly takes place in correspondenc...
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| Veröffentlicht in: | EMBO reports 2016-09, Vol.17 (9), p.1264-1280 |
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| creator | Doghman-Bouguerra, Mabrouka Granatiero, Veronica Sbiera, Silviu Sbiera, Iuliu Lacas-Gervais, Sandra Brau, Frédéric Fassnacht, Martin Rizzuto, Rosario Lalli, Enzo |
| description | Several stimuli induce programmed cell death by increasing Ca
2+
transfer from the endoplasmic reticulum (ER) to mitochondria. Perturbation of this process has a special relevance in pathologies as cancer and neurodegenerative disorders. Mitochondrial Ca
2+
uptake mainly takes place in correspondence of mitochondria‐associated ER membranes (MAM), specialized contact sites between the two organelles. Here, we show the important role of FATE1, a cancer‐testis antigen, in the regulation of ER–mitochondria distance and Ca
2+
uptake by mitochondria. FATE1 is localized at the interface between ER and mitochondria, fractionating into MAM. FATE1 expression in adrenocortical carcinoma (ACC) cells under the control of the transcription factor SF‐1 decreases ER–mitochondria contact and mitochondrial Ca
2+
uptake, while its knockdown has an opposite effect. FATE1 also decreases sensitivity to mitochondrial Ca
2+
‐dependent pro‐apoptotic stimuli and to the chemotherapeutic drug mitotane. In patients with ACC, FATE1 expression in their tumor is inversely correlated with their overall survival. These results show that the ER–mitochondria uncoupling activity of FATE1 is harnessed by cancer cells to escape apoptotic death and resist the action of chemotherapeutic drugs.
Synopsis
This study shows that FATE1, a cancer‐testis antigen, is localized at the interface between the ER and mitochondria where it modulates the coupling of the two organelles and apoptotic cell death.
FATE1 is a cancer‐testis antigen.
FATE1 levels are a prognostic indicator in adrenocortical carcinoma patients.
Graphical Abstract
This study shows that FATE1, a cancer‐testis antigen, is localized at the interface between the ER and mitochondria where it modulates the coupling of the two organelles and apoptotic cell death. |
| doi_str_mv | 10.15252/embr.201541504 |
| format | Article |
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2+
transfer from the endoplasmic reticulum (ER) to mitochondria. Perturbation of this process has a special relevance in pathologies as cancer and neurodegenerative disorders. Mitochondrial Ca
2+
uptake mainly takes place in correspondence of mitochondria‐associated ER membranes (MAM), specialized contact sites between the two organelles. Here, we show the important role of FATE1, a cancer‐testis antigen, in the regulation of ER–mitochondria distance and Ca
2+
uptake by mitochondria. FATE1 is localized at the interface between ER and mitochondria, fractionating into MAM. FATE1 expression in adrenocortical carcinoma (ACC) cells under the control of the transcription factor SF‐1 decreases ER–mitochondria contact and mitochondrial Ca
2+
uptake, while its knockdown has an opposite effect. FATE1 also decreases sensitivity to mitochondrial Ca
2+
‐dependent pro‐apoptotic stimuli and to the chemotherapeutic drug mitotane. In patients with ACC, FATE1 expression in their tumor is inversely correlated with their overall survival. These results show that the ER–mitochondria uncoupling activity of FATE1 is harnessed by cancer cells to escape apoptotic death and resist the action of chemotherapeutic drugs.
Synopsis
This study shows that FATE1, a cancer‐testis antigen, is localized at the interface between the ER and mitochondria where it modulates the coupling of the two organelles and apoptotic cell death.
FATE1 is a cancer‐testis antigen.
FATE1 levels are a prognostic indicator in adrenocortical carcinoma patients.
Graphical Abstract
This study shows that FATE1, a cancer‐testis antigen, is localized at the interface between the ER and mitochondria where it modulates the coupling of the two organelles and apoptotic cell death.</description><identifier>ISSN: 1469-221X</identifier><identifier>EISSN: 1469-3178</identifier><identifier>DOI: 10.15252/embr.201541504</identifier><identifier>PMID: 27402544</identifier><identifier>CODEN: ERMEAX</identifier><language>eng</language><publisher>London: Blackwell Publishing Ltd</publisher><subject>adrenal cortex ; Adrenocortical Carcinoma - genetics ; Adrenocortical Carcinoma - metabolism ; Adrenocortical Carcinoma - mortality ; Antigens ; Antineoplastic Agents, Hormonal - pharmacology ; Apoptosis ; Apoptosis - drug effects ; Biochemistry, Molecular Biology ; Calcium ; Calcium - metabolism ; Cancer ; Cellular Biology ; Chemotherapy ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; EMBO07 ; endocrine cancer ; Endoplasmic reticulum ; Endoplasmic Reticulum - metabolism ; Endoplasmic Reticulum - ultrastructure ; Gene Expression ; Humans ; Life Sciences ; MAM ; Membrane Potential, Mitochondrial ; Mitochondria ; Mitochondria - metabolism ; Mitochondria - ultrastructure ; Mitochondrial Membranes - metabolism ; Mitotane - pharmacology ; Mortality ; Prognosis ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Transport ; Scientific Report ; Scientific Reports ; Steroids - pharmacology ; Transcription Factors - chemistry ; Transcription Factors - genetics ; Transcription Factors - metabolism</subject><ispartof>EMBO reports, 2016-09, Vol.17 (9), p.1264-1280</ispartof><rights>The Authors 2016</rights><rights>2016 The Authors</rights><rights>2016 The Authors.</rights><rights>2016 EMBO</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><orcidid>0000-0002-0584-5681 ; 0000-0001-5967-5895 ; 0000-0001-5112-7755 ; 0000-0001-6170-6398</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/PMC5007562/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5007562/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27923,27924,41119,42188,45573,45574,46408,46832,51575,53790,53792</link.rule.ids><linktorsrc>$$Uhttps://doi.org/10.15252/embr.201541504$$EView_record_in_Springer_Nature$$FView_record_in_$$GSpringer_Nature</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27402544$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-02108682$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Doghman-Bouguerra, Mabrouka</creatorcontrib><creatorcontrib>Granatiero, Veronica</creatorcontrib><creatorcontrib>Sbiera, Silviu</creatorcontrib><creatorcontrib>Sbiera, Iuliu</creatorcontrib><creatorcontrib>Lacas-Gervais, Sandra</creatorcontrib><creatorcontrib>Brau, Frédéric</creatorcontrib><creatorcontrib>Fassnacht, Martin</creatorcontrib><creatorcontrib>Rizzuto, Rosario</creatorcontrib><creatorcontrib>Lalli, Enzo</creatorcontrib><title>FATE1 antagonizes calcium- and drug-induced apoptosis by uncoupling ER and mitochondria</title><title>EMBO reports</title><addtitle>EMBO Rep</addtitle><addtitle>EMBO rep</addtitle><description>Several stimuli induce programmed cell death by increasing Ca
2+
transfer from the endoplasmic reticulum (ER) to mitochondria. Perturbation of this process has a special relevance in pathologies as cancer and neurodegenerative disorders. Mitochondrial Ca
2+
uptake mainly takes place in correspondence of mitochondria‐associated ER membranes (MAM), specialized contact sites between the two organelles. Here, we show the important role of FATE1, a cancer‐testis antigen, in the regulation of ER–mitochondria distance and Ca
2+
uptake by mitochondria. FATE1 is localized at the interface between ER and mitochondria, fractionating into MAM. FATE1 expression in adrenocortical carcinoma (ACC) cells under the control of the transcription factor SF‐1 decreases ER–mitochondria contact and mitochondrial Ca
2+
uptake, while its knockdown has an opposite effect. FATE1 also decreases sensitivity to mitochondrial Ca
2+
‐dependent pro‐apoptotic stimuli and to the chemotherapeutic drug mitotane. In patients with ACC, FATE1 expression in their tumor is inversely correlated with their overall survival. These results show that the ER–mitochondria uncoupling activity of FATE1 is harnessed by cancer cells to escape apoptotic death and resist the action of chemotherapeutic drugs.
Synopsis
This study shows that FATE1, a cancer‐testis antigen, is localized at the interface between the ER and mitochondria where it modulates the coupling of the two organelles and apoptotic cell death.
FATE1 is a cancer‐testis antigen.
FATE1 levels are a prognostic indicator in adrenocortical carcinoma patients.
Graphical Abstract
This study shows that FATE1, a cancer‐testis antigen, is localized at the interface between the ER and mitochondria where it modulates the coupling of the two organelles and apoptotic cell death.</description><subject>adrenal cortex</subject><subject>Adrenocortical Carcinoma - genetics</subject><subject>Adrenocortical Carcinoma - metabolism</subject><subject>Adrenocortical Carcinoma - mortality</subject><subject>Antigens</subject><subject>Antineoplastic Agents, Hormonal - pharmacology</subject><subject>Apoptosis</subject><subject>Apoptosis - drug effects</subject><subject>Biochemistry, Molecular Biology</subject><subject>Calcium</subject><subject>Calcium - metabolism</subject><subject>Cancer</subject><subject>Cellular Biology</subject><subject>Chemotherapy</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>EMBO07</subject><subject>endocrine cancer</subject><subject>Endoplasmic reticulum</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Endoplasmic Reticulum - ultrastructure</subject><subject>Gene Expression</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>MAM</subject><subject>Membrane Potential, Mitochondrial</subject><subject>Mitochondria</subject><subject>Mitochondria - metabolism</subject><subject>Mitochondria - ultrastructure</subject><subject>Mitochondrial Membranes - metabolism</subject><subject>Mitotane - pharmacology</subject><subject>Mortality</subject><subject>Prognosis</subject><subject>Protein Binding</subject><subject>Protein Interaction Domains and Motifs</subject><subject>Protein Transport</subject><subject>Scientific Report</subject><subject>Scientific Reports</subject><subject>Steroids - pharmacology</subject><subject>Transcription Factors - chemistry</subject><subject>Transcription Factors - genetics</subject><subject>Transcription Factors - metabolism</subject><issn>1469-221X</issn><issn>1469-3178</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkc1v1DAQxSMEoqVw5oYicYFDir_GcThU2lbbLdIWpKqo3CzHcbIuiR3ipLD89WSbJSoVJ9szv_feyBNFrzE6xkCAfDBN3h0ThIFhQOxJdIgZzxKKU_F0fycEfzuIXoRwixCCLBXPowOSMkSAscPo5nxxvcSxcr2qvLO_TYi1qrUdmmQsFnHRDVViXTFoU8Sq9W3vgw1xvo0Hp_3Q1tZV8fLqnm1s7_XGu6Kz6mX0rFR1MK_251H09Xx5fXaRrL-sPp0t1smGgWCJKgwQhAg1Wa61QEZphjhNGSCBIWeGg2aiLDErDDW8LEpEMyAZgFGCc6BH0cnk2w55YwptXN-pWradbVS3lV5Z-W_H2Y2s_J0EhFLgZDR4PxlsHskuFmu5qyGCkeCC3OGRfbcP6_yPwYReNjZoU9fKGT8EiQXmnAIlO_TtI_TWD50bv2JH7YIBxEi9eTj9nP93PyPwcQJ-2tps5z5G8n79crd-Oa9fLi9Pr-bXKEaTOIw6V5nuwQz_NxglySSxoTe_5jzVfZc8pSnIm88reUkyRk9XQmL6BxT0wOo</recordid><startdate>201609</startdate><enddate>201609</enddate><creator>Doghman-Bouguerra, Mabrouka</creator><creator>Granatiero, Veronica</creator><creator>Sbiera, Silviu</creator><creator>Sbiera, Iuliu</creator><creator>Lacas-Gervais, Sandra</creator><creator>Brau, Frédéric</creator><creator>Fassnacht, Martin</creator><creator>Rizzuto, Rosario</creator><creator>Lalli, Enzo</creator><general>Blackwell Publishing Ltd</general><general>Nature Publishing Group UK</general><general>EMBO Press</general><general>John Wiley and Sons Inc</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>7T5</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>1XC</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-0584-5681</orcidid><orcidid>https://orcid.org/0000-0001-5967-5895</orcidid><orcidid>https://orcid.org/0000-0001-5112-7755</orcidid><orcidid>https://orcid.org/0000-0001-6170-6398</orcidid></search><sort><creationdate>201609</creationdate><title>FATE1 antagonizes calcium- and drug-induced apoptosis by uncoupling ER and mitochondria</title><author>Doghman-Bouguerra, Mabrouka ; Granatiero, Veronica ; Sbiera, Silviu ; Sbiera, Iuliu ; Lacas-Gervais, Sandra ; Brau, Frédéric ; Fassnacht, Martin ; Rizzuto, Rosario ; Lalli, Enzo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h4584-ade520023e9bcc80eac40637450815b4e65c48ff14de3e6fdf03952955ea86653</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>adrenal cortex</topic><topic>Adrenocortical Carcinoma - genetics</topic><topic>Adrenocortical Carcinoma - metabolism</topic><topic>Adrenocortical Carcinoma - mortality</topic><topic>Antigens</topic><topic>Antineoplastic Agents, Hormonal - pharmacology</topic><topic>Apoptosis</topic><topic>Apoptosis - drug effects</topic><topic>Biochemistry, Molecular Biology</topic><topic>Calcium</topic><topic>Calcium - metabolism</topic><topic>Cancer</topic><topic>Cellular Biology</topic><topic>Chemotherapy</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>EMBO07</topic><topic>endocrine cancer</topic><topic>Endoplasmic reticulum</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Endoplasmic Reticulum - ultrastructure</topic><topic>Gene Expression</topic><topic>Humans</topic><topic>Life Sciences</topic><topic>MAM</topic><topic>Membrane Potential, Mitochondrial</topic><topic>Mitochondria</topic><topic>Mitochondria - metabolism</topic><topic>Mitochondria - ultrastructure</topic><topic>Mitochondrial Membranes - metabolism</topic><topic>Mitotane - pharmacology</topic><topic>Mortality</topic><topic>Prognosis</topic><topic>Protein Binding</topic><topic>Protein Interaction Domains and Motifs</topic><topic>Protein Transport</topic><topic>Scientific Report</topic><topic>Scientific Reports</topic><topic>Steroids - pharmacology</topic><topic>Transcription Factors - chemistry</topic><topic>Transcription Factors - genetics</topic><topic>Transcription Factors - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Doghman-Bouguerra, Mabrouka</creatorcontrib><creatorcontrib>Granatiero, Veronica</creatorcontrib><creatorcontrib>Sbiera, Silviu</creatorcontrib><creatorcontrib>Sbiera, Iuliu</creatorcontrib><creatorcontrib>Lacas-Gervais, Sandra</creatorcontrib><creatorcontrib>Brau, Frédéric</creatorcontrib><creatorcontrib>Fassnacht, Martin</creatorcontrib><creatorcontrib>Rizzuto, Rosario</creatorcontrib><creatorcontrib>Lalli, Enzo</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>EMBO reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Doghman-Bouguerra, Mabrouka</au><au>Granatiero, Veronica</au><au>Sbiera, Silviu</au><au>Sbiera, Iuliu</au><au>Lacas-Gervais, Sandra</au><au>Brau, Frédéric</au><au>Fassnacht, Martin</au><au>Rizzuto, Rosario</au><au>Lalli, Enzo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>FATE1 antagonizes calcium- and drug-induced apoptosis by uncoupling ER and mitochondria</atitle><jtitle>EMBO reports</jtitle><stitle>EMBO Rep</stitle><addtitle>EMBO rep</addtitle><date>2016-09</date><risdate>2016</risdate><volume>17</volume><issue>9</issue><spage>1264</spage><epage>1280</epage><pages>1264-1280</pages><issn>1469-221X</issn><eissn>1469-3178</eissn><coden>ERMEAX</coden><abstract>Several stimuli induce programmed cell death by increasing Ca
2+
transfer from the endoplasmic reticulum (ER) to mitochondria. Perturbation of this process has a special relevance in pathologies as cancer and neurodegenerative disorders. Mitochondrial Ca
2+
uptake mainly takes place in correspondence of mitochondria‐associated ER membranes (MAM), specialized contact sites between the two organelles. Here, we show the important role of FATE1, a cancer‐testis antigen, in the regulation of ER–mitochondria distance and Ca
2+
uptake by mitochondria. FATE1 is localized at the interface between ER and mitochondria, fractionating into MAM. FATE1 expression in adrenocortical carcinoma (ACC) cells under the control of the transcription factor SF‐1 decreases ER–mitochondria contact and mitochondrial Ca
2+
uptake, while its knockdown has an opposite effect. FATE1 also decreases sensitivity to mitochondrial Ca
2+
‐dependent pro‐apoptotic stimuli and to the chemotherapeutic drug mitotane. In patients with ACC, FATE1 expression in their tumor is inversely correlated with their overall survival. These results show that the ER–mitochondria uncoupling activity of FATE1 is harnessed by cancer cells to escape apoptotic death and resist the action of chemotherapeutic drugs.
Synopsis
This study shows that FATE1, a cancer‐testis antigen, is localized at the interface between the ER and mitochondria where it modulates the coupling of the two organelles and apoptotic cell death.
FATE1 is a cancer‐testis antigen.
FATE1 levels are a prognostic indicator in adrenocortical carcinoma patients.
Graphical Abstract
This study shows that FATE1, a cancer‐testis antigen, is localized at the interface between the ER and mitochondria where it modulates the coupling of the two organelles and apoptotic cell death.</abstract><cop>London</cop><pub>Blackwell Publishing Ltd</pub><pmid>27402544</pmid><doi>10.15252/embr.201541504</doi><tpages>17</tpages><orcidid>https://orcid.org/0000-0002-0584-5681</orcidid><orcidid>https://orcid.org/0000-0001-5967-5895</orcidid><orcidid>https://orcid.org/0000-0001-5112-7755</orcidid><orcidid>https://orcid.org/0000-0001-6170-6398</orcidid><oa>free_for_read</oa></addata></record> |
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| source | Springer Nature OA/Free Journals |
| subjects | adrenal cortex Adrenocortical Carcinoma - genetics Adrenocortical Carcinoma - metabolism Adrenocortical Carcinoma - mortality Antigens Antineoplastic Agents, Hormonal - pharmacology Apoptosis Apoptosis - drug effects Biochemistry, Molecular Biology Calcium Calcium - metabolism Cancer Cellular Biology Chemotherapy DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism EMBO07 endocrine cancer Endoplasmic reticulum Endoplasmic Reticulum - metabolism Endoplasmic Reticulum - ultrastructure Gene Expression Humans Life Sciences MAM Membrane Potential, Mitochondrial Mitochondria Mitochondria - metabolism Mitochondria - ultrastructure Mitochondrial Membranes - metabolism Mitotane - pharmacology Mortality Prognosis Protein Binding Protein Interaction Domains and Motifs Protein Transport Scientific Report Scientific Reports Steroids - pharmacology Transcription Factors - chemistry Transcription Factors - genetics Transcription Factors - metabolism |
| title | FATE1 antagonizes calcium- and drug-induced apoptosis by uncoupling ER and mitochondria |
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