Regulation of cytoplasmic stress granules by apoptosis-inducing factor
Stress granules (SG) are dynamic cytoplasmic foci in which stalled translation initiation complexes accumulate. In conditions of acute cellular redox, stress cells manipulated to lose the expression of apoptosis-inducing factor (AIF) nucleate SG signature proteins (e.g. TIA-1, PABP1) more efficientl...
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| Veröffentlicht in: | Journal of cell science 2004-09, Vol.117 (Pt 19), p.4461-4468 |
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| container_issue | Pt 19 |
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| container_title | Journal of cell science |
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| creator | Candé, Céline Vahsen, Nicola Métivier, Didier Tourrière, Hélène Chebli, Karim Garrido, Carmen Tazi, Jamal Kroemer, Guido |
| description | Stress granules (SG) are dynamic cytoplasmic foci in which stalled translation initiation complexes accumulate. In conditions of acute cellular redox, stress cells manipulated to lose the expression of apoptosis-inducing factor (AIF) nucleate SG signature proteins (e.g. TIA-1, PABP1) more efficiently than AIF-positive controls. AIF also inhibited SG formation induced by the RasGAP-associated endoribonuclease G3BP. Retransfection of mouse AIF into cells subjected to human AIF-specific siRNA revealed that only AIF imported into mitochondria could repress SGs and that redox-active domains of AIF, which are dispensable for its apoptogenic action, were required for SG inhibition. In response to oxidative stress, AIF-negative cells were found to deplete non-oxidized glutathione more rapidly than AIF-expressing cells. Exogenous supplementation of glutathione inhibited SG formation elicited by arsenate or G3BP. Together, these data suggest that the oxidoreductase function of AIF is required for the maintenance of glutathione levels in stress conditions and that glutathione is a major regulator of SG. |
| doi_str_mv | 10.1242/jcs.01356 |
| format | Article |
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In conditions of acute cellular redox, stress cells manipulated to lose the expression of apoptosis-inducing factor (AIF) nucleate SG signature proteins (e.g. TIA-1, PABP1) more efficiently than AIF-positive controls. AIF also inhibited SG formation induced by the RasGAP-associated endoribonuclease G3BP. Retransfection of mouse AIF into cells subjected to human AIF-specific siRNA revealed that only AIF imported into mitochondria could repress SGs and that redox-active domains of AIF, which are dispensable for its apoptogenic action, were required for SG inhibition. In response to oxidative stress, AIF-negative cells were found to deplete non-oxidized glutathione more rapidly than AIF-expressing cells. Exogenous supplementation of glutathione inhibited SG formation elicited by arsenate or G3BP. Together, these data suggest that the oxidoreductase function of AIF is required for the maintenance of glutathione levels in stress conditions and that glutathione is a major regulator of SG.</description><identifier>ISSN: 0021-9533</identifier><identifier>EISSN: 1477-9137</identifier><identifier>DOI: 10.1242/jcs.01356</identifier><identifier>PMID: 15316071</identifier><language>eng</language><publisher>England: Company of Biologists</publisher><subject>Acetylcysteine - toxicity ; Apoptosis - drug effects ; Apoptosis - physiology ; Apoptosis Inducing Factor ; Arsenates - toxicity ; Biochemistry, Molecular Biology ; Carrier Proteins - metabolism ; DNA Helicases ; Flavoproteins - metabolism ; Glutathione - analogs & derivatives ; Glutathione - metabolism ; Glutathione - toxicity ; HeLa Cells ; Humans ; Life Sciences ; Membrane Proteins - metabolism ; Mitochondria - drug effects ; Mitochondria - metabolism ; Organelles - drug effects ; Organelles - metabolism ; Oxidation-Reduction - drug effects ; Poly-ADP-Ribose Binding Proteins ; Protein Transport - drug effects ; Protein Transport - physiology ; RNA Helicases ; RNA Recognition Motif Proteins ; RNA, Small Interfering - metabolism</subject><ispartof>Journal of cell science, 2004-09, Vol.117 (Pt 19), p.4461-4468</ispartof><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c484t-20d7239cc4fa6505b4e1903c7cfda15d276f55d9f51c23259f2d894f38d581a3</citedby><cites>FETCH-LOGICAL-c484t-20d7239cc4fa6505b4e1903c7cfda15d276f55d9f51c23259f2d894f38d581a3</cites><orcidid>0000-0002-9334-4405</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,3676,27922,27923</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15316071$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-02262401$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Candé, Céline</creatorcontrib><creatorcontrib>Vahsen, Nicola</creatorcontrib><creatorcontrib>Métivier, Didier</creatorcontrib><creatorcontrib>Tourrière, Hélène</creatorcontrib><creatorcontrib>Chebli, Karim</creatorcontrib><creatorcontrib>Garrido, Carmen</creatorcontrib><creatorcontrib>Tazi, Jamal</creatorcontrib><creatorcontrib>Kroemer, Guido</creatorcontrib><title>Regulation of cytoplasmic stress granules by apoptosis-inducing factor</title><title>Journal of cell science</title><addtitle>J Cell Sci</addtitle><description>Stress granules (SG) are dynamic cytoplasmic foci in which stalled translation initiation complexes accumulate. In conditions of acute cellular redox, stress cells manipulated to lose the expression of apoptosis-inducing factor (AIF) nucleate SG signature proteins (e.g. TIA-1, PABP1) more efficiently than AIF-positive controls. AIF also inhibited SG formation induced by the RasGAP-associated endoribonuclease G3BP. Retransfection of mouse AIF into cells subjected to human AIF-specific siRNA revealed that only AIF imported into mitochondria could repress SGs and that redox-active domains of AIF, which are dispensable for its apoptogenic action, were required for SG inhibition. In response to oxidative stress, AIF-negative cells were found to deplete non-oxidized glutathione more rapidly than AIF-expressing cells. Exogenous supplementation of glutathione inhibited SG formation elicited by arsenate or G3BP. Together, these data suggest that the oxidoreductase function of AIF is required for the maintenance of glutathione levels in stress conditions and that glutathione is a major regulator of SG.</description><subject>Acetylcysteine - toxicity</subject><subject>Apoptosis - drug effects</subject><subject>Apoptosis - physiology</subject><subject>Apoptosis Inducing Factor</subject><subject>Arsenates - toxicity</subject><subject>Biochemistry, Molecular Biology</subject><subject>Carrier Proteins - metabolism</subject><subject>DNA Helicases</subject><subject>Flavoproteins - metabolism</subject><subject>Glutathione - analogs & derivatives</subject><subject>Glutathione - metabolism</subject><subject>Glutathione - toxicity</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Membrane Proteins - metabolism</subject><subject>Mitochondria - drug effects</subject><subject>Mitochondria - metabolism</subject><subject>Organelles - drug effects</subject><subject>Organelles - metabolism</subject><subject>Oxidation-Reduction - drug effects</subject><subject>Poly-ADP-Ribose Binding Proteins</subject><subject>Protein Transport - drug effects</subject><subject>Protein Transport - physiology</subject><subject>RNA Helicases</subject><subject>RNA Recognition Motif Proteins</subject><subject>RNA, Small Interfering - metabolism</subject><issn>0021-9533</issn><issn>1477-9137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkE1LwzAch4Mobk4PfgHpSfDQmX9emuY4xDlhIMjuIcvLzGib2rTCvr2bG-70gx8Pz-FB6B7wFAgjz1uTphgoLy7QGJgQuQQqLtEYYwK55JSO0E1KW4yxIFJcoxFwCgUWMEbzT7cZKt2H2GTRZ2bXx7bSqQ4mS33nUso2nW6GyqVsvct0G9s-ppDy0NjBhGaTeW362N2iK6-r5O5OO0Gr-evqZZEvP97eX2bL3LCS9TnBVhAqjWFeFxzzNXMgMTXCeKuBWyIKz7mVnoMhlHDpiS0l87S0vARNJ-jpqP3SlWq7UOtup6IOajFbqsOHCSkIw_ADe_bxyLZd_B5c6lUdknFVpRsXh6SgxIRSYGep6WJKnfP_ZsDq0Fft-6q_vnv24SQd1rWzZ_IUlP4Cy091IA</recordid><startdate>20040901</startdate><enddate>20040901</enddate><creator>Candé, Céline</creator><creator>Vahsen, Nicola</creator><creator>Métivier, Didier</creator><creator>Tourrière, Hélène</creator><creator>Chebli, Karim</creator><creator>Garrido, Carmen</creator><creator>Tazi, Jamal</creator><creator>Kroemer, Guido</creator><general>Company of Biologists</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>7TM</scope><scope>1XC</scope><scope>VOOES</scope><orcidid>https://orcid.org/0000-0002-9334-4405</orcidid></search><sort><creationdate>20040901</creationdate><title>Regulation of cytoplasmic stress granules by apoptosis-inducing factor</title><author>Candé, Céline ; Vahsen, Nicola ; Métivier, Didier ; Tourrière, Hélène ; Chebli, Karim ; Garrido, Carmen ; Tazi, Jamal ; Kroemer, Guido</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c484t-20d7239cc4fa6505b4e1903c7cfda15d276f55d9f51c23259f2d894f38d581a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Acetylcysteine - toxicity</topic><topic>Apoptosis - drug effects</topic><topic>Apoptosis - physiology</topic><topic>Apoptosis Inducing Factor</topic><topic>Arsenates - toxicity</topic><topic>Biochemistry, Molecular Biology</topic><topic>Carrier Proteins - metabolism</topic><topic>DNA Helicases</topic><topic>Flavoproteins - metabolism</topic><topic>Glutathione - analogs & derivatives</topic><topic>Glutathione - metabolism</topic><topic>Glutathione - toxicity</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Life Sciences</topic><topic>Membrane Proteins - metabolism</topic><topic>Mitochondria - drug effects</topic><topic>Mitochondria - metabolism</topic><topic>Organelles - drug effects</topic><topic>Organelles - metabolism</topic><topic>Oxidation-Reduction - drug effects</topic><topic>Poly-ADP-Ribose Binding Proteins</topic><topic>Protein Transport - drug effects</topic><topic>Protein Transport - physiology</topic><topic>RNA Helicases</topic><topic>RNA Recognition Motif Proteins</topic><topic>RNA, Small Interfering - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Candé, Céline</creatorcontrib><creatorcontrib>Vahsen, Nicola</creatorcontrib><creatorcontrib>Métivier, Didier</creatorcontrib><creatorcontrib>Tourrière, Hélène</creatorcontrib><creatorcontrib>Chebli, Karim</creatorcontrib><creatorcontrib>Garrido, Carmen</creatorcontrib><creatorcontrib>Tazi, Jamal</creatorcontrib><creatorcontrib>Kroemer, Guido</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><jtitle>Journal of cell science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Candé, Céline</au><au>Vahsen, Nicola</au><au>Métivier, Didier</au><au>Tourrière, Hélène</au><au>Chebli, Karim</au><au>Garrido, Carmen</au><au>Tazi, Jamal</au><au>Kroemer, Guido</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of cytoplasmic stress granules by apoptosis-inducing factor</atitle><jtitle>Journal of cell science</jtitle><addtitle>J Cell Sci</addtitle><date>2004-09-01</date><risdate>2004</risdate><volume>117</volume><issue>Pt 19</issue><spage>4461</spage><epage>4468</epage><pages>4461-4468</pages><issn>0021-9533</issn><eissn>1477-9137</eissn><abstract>Stress granules (SG) are dynamic cytoplasmic foci in which stalled translation initiation complexes accumulate. In conditions of acute cellular redox, stress cells manipulated to lose the expression of apoptosis-inducing factor (AIF) nucleate SG signature proteins (e.g. TIA-1, PABP1) more efficiently than AIF-positive controls. AIF also inhibited SG formation induced by the RasGAP-associated endoribonuclease G3BP. Retransfection of mouse AIF into cells subjected to human AIF-specific siRNA revealed that only AIF imported into mitochondria could repress SGs and that redox-active domains of AIF, which are dispensable for its apoptogenic action, were required for SG inhibition. In response to oxidative stress, AIF-negative cells were found to deplete non-oxidized glutathione more rapidly than AIF-expressing cells. Exogenous supplementation of glutathione inhibited SG formation elicited by arsenate or G3BP. Together, these data suggest that the oxidoreductase function of AIF is required for the maintenance of glutathione levels in stress conditions and that glutathione is a major regulator of SG.</abstract><cop>England</cop><pub>Company of Biologists</pub><pmid>15316071</pmid><doi>10.1242/jcs.01356</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0002-9334-4405</orcidid><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Company of Biologists |
| subjects | Acetylcysteine - toxicity Apoptosis - drug effects Apoptosis - physiology Apoptosis Inducing Factor Arsenates - toxicity Biochemistry, Molecular Biology Carrier Proteins - metabolism DNA Helicases Flavoproteins - metabolism Glutathione - analogs & derivatives Glutathione - metabolism Glutathione - toxicity HeLa Cells Humans Life Sciences Membrane Proteins - metabolism Mitochondria - drug effects Mitochondria - metabolism Organelles - drug effects Organelles - metabolism Oxidation-Reduction - drug effects Poly-ADP-Ribose Binding Proteins Protein Transport - drug effects Protein Transport - physiology RNA Helicases RNA Recognition Motif Proteins RNA, Small Interfering - metabolism |
| title | Regulation of cytoplasmic stress granules by apoptosis-inducing factor |
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