The mitochondrial fission factor dynamin-related protein 1 modulates T-cell receptor signalling at the immune synapse
During antigen‐specific T‐cell activation, mitochondria mobilize towards the vicinity of the immune synapse. We show here that the mitochondrial fission factor dynamin‐related protein 1 (Drp1) docks at mitochondria, regulating their positioning and activity near the actin‐rich ring of the peripheral...
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| Veröffentlicht in: | The EMBO journal 2011-04, Vol.30 (7), p.1238-1250 |
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| creator | Baixauli, Francesc Martín-Cófreces, Noa B Morlino, Giulia Carrasco, Yolanda R Calabia-Linares, Carmen Veiga, Esteban Serrador, Juan M Sánchez-Madrid, Francisco |
| description | During antigen‐specific T‐cell activation, mitochondria mobilize towards the vicinity of the immune synapse. We show here that the mitochondrial fission factor dynamin‐related protein 1 (Drp1) docks at mitochondria, regulating their positioning and activity near the actin‐rich ring of the peripheral supramolecular activation cluster (pSMAC) of the immune synapse. Mitochondrial redistribution in response to T‐cell receptor engagement was abolished by Drp1 silencing, expression of the phosphomimetic mutant Drp1S637D and the Drp1‐specific inhibitor mdivi‐1. Moreover, Drp1 knockdown enhanced mitochondrial depolarization and T‐cell receptor signal strength, but decreased myosin phosphorylation, ATP production and T‐cell receptor assembly at the central supramolecular activation cluster (cSMAC). Our results indicate that Drp1‐dependent mitochondrial positioning and activity controls T‐cell activation by fuelling central supramolecular activation cluster assembly at the immune synapse.
During antigen presentation, T cells relocalize organelles, adhesion and signalling components to the immunological synapse (IS). This study shows that the localization of mitochondria to the IS is regulated by the mitochondrial fission factor Drp1 and that this is important for T‐cell activation. |
| doi_str_mv | 10.1038/emboj.2011.25 |
| format | Article |
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During antigen presentation, T cells relocalize organelles, adhesion and signalling components to the immunological synapse (IS). This study shows that the localization of mitochondria to the IS is regulated by the mitochondrial fission factor Drp1 and that this is important for T‐cell activation.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1038/emboj.2011.25</identifier><identifier>PMID: 21326213</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Antigens ; ATP ; cell signalling ; Cells ; Docks ; EMBO19 ; EMBO40 ; fission factor ; Gene Silencing ; GTP Phosphohydrolases - antagonists & inhibitors ; GTP Phosphohydrolases - genetics ; GTP Phosphohydrolases - metabolism ; Humans ; immune synapse ; Immune system ; Immunological Synapses - physiology ; Immunological Synapses - ultrastructure ; Lymphocytes - physiology ; Microtubule-Associated Proteins - antagonists & inhibitors ; Microtubule-Associated Proteins - genetics ; Microtubule-Associated Proteins - metabolism ; mitochondria ; Mitochondria - metabolism ; Mitochondria - ultrastructure ; Mitochondrial Proteins - antagonists & inhibitors ; Mitochondrial Proteins - genetics ; Mitochondrial Proteins - metabolism ; Mutant Proteins - genetics ; Mutant Proteins - metabolism ; Mutation, Missense ; Neurons ; Proteins ; Receptors, Antigen, T-Cell - metabolism ; T-cell receptor</subject><ispartof>The EMBO journal, 2011-04, Vol.30 (7), p.1238-1250</ispartof><rights>European Molecular Biology Organization 2011</rights><rights>Copyright © 2011 European Molecular Biology Organization</rights><rights>Copyright Nature Publishing Group Apr 6, 2011</rights><rights>Copyright © 2011, European Molecular Biology Organization 2011 European Molecular Biology Organization</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5565-5db8fe4043ad1586e5e0380d53672ba80f795574779d976cc97fb7c2759266cb3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3094108/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3094108/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,41120,42189,45574,45575,46409,46833,51576,53791,53793</link.rule.ids><linktorsrc>$$Uhttps://doi.org/10.1038/emboj.2011.25$$EView_record_in_Springer_Nature$$FView_record_in_$$GSpringer_Nature</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21326213$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Baixauli, Francesc</creatorcontrib><creatorcontrib>Martín-Cófreces, Noa B</creatorcontrib><creatorcontrib>Morlino, Giulia</creatorcontrib><creatorcontrib>Carrasco, Yolanda R</creatorcontrib><creatorcontrib>Calabia-Linares, Carmen</creatorcontrib><creatorcontrib>Veiga, Esteban</creatorcontrib><creatorcontrib>Serrador, Juan M</creatorcontrib><creatorcontrib>Sánchez-Madrid, Francisco</creatorcontrib><title>The mitochondrial fission factor dynamin-related protein 1 modulates T-cell receptor signalling at the immune synapse</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>During antigen‐specific T‐cell activation, mitochondria mobilize towards the vicinity of the immune synapse. We show here that the mitochondrial fission factor dynamin‐related protein 1 (Drp1) docks at mitochondria, regulating their positioning and activity near the actin‐rich ring of the peripheral supramolecular activation cluster (pSMAC) of the immune synapse. Mitochondrial redistribution in response to T‐cell receptor engagement was abolished by Drp1 silencing, expression of the phosphomimetic mutant Drp1S637D and the Drp1‐specific inhibitor mdivi‐1. Moreover, Drp1 knockdown enhanced mitochondrial depolarization and T‐cell receptor signal strength, but decreased myosin phosphorylation, ATP production and T‐cell receptor assembly at the central supramolecular activation cluster (cSMAC). Our results indicate that Drp1‐dependent mitochondrial positioning and activity controls T‐cell activation by fuelling central supramolecular activation cluster assembly at the immune synapse.
During antigen presentation, T cells relocalize organelles, adhesion and signalling components to the immunological synapse (IS). This study shows that the localization of mitochondria to the IS is regulated by the mitochondrial fission factor Drp1 and that this is important for T‐cell activation.</description><subject>Antigens</subject><subject>ATP</subject><subject>cell signalling</subject><subject>Cells</subject><subject>Docks</subject><subject>EMBO19</subject><subject>EMBO40</subject><subject>fission factor</subject><subject>Gene Silencing</subject><subject>GTP Phosphohydrolases - antagonists & inhibitors</subject><subject>GTP Phosphohydrolases - genetics</subject><subject>GTP Phosphohydrolases - metabolism</subject><subject>Humans</subject><subject>immune synapse</subject><subject>Immune system</subject><subject>Immunological Synapses - physiology</subject><subject>Immunological Synapses - ultrastructure</subject><subject>Lymphocytes - physiology</subject><subject>Microtubule-Associated Proteins - antagonists & inhibitors</subject><subject>Microtubule-Associated Proteins - genetics</subject><subject>Microtubule-Associated Proteins - metabolism</subject><subject>mitochondria</subject><subject>Mitochondria - metabolism</subject><subject>Mitochondria - ultrastructure</subject><subject>Mitochondrial Proteins - antagonists & inhibitors</subject><subject>Mitochondrial Proteins - genetics</subject><subject>Mitochondrial Proteins - metabolism</subject><subject>Mutant Proteins - genetics</subject><subject>Mutant Proteins - metabolism</subject><subject>Mutation, Missense</subject><subject>Neurons</subject><subject>Proteins</subject><subject>Receptors, Antigen, T-Cell - metabolism</subject><subject>T-cell receptor</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkk1v1DAQhiMEokvhyBUZLpyy2E78kQtSqUoBFRCwiKPlJJNdL4kd7ATYf4-zKeFDSFxsy_O878zYkyT3CV4TnMkn0JVuv6aYkDVlN5IVyTlOKRbsZrLClJM0J7I4Se6EsMcYMynI7eSEkozyuKyScbMD1JnBVTtna290ixoTgnEWNboanEf1werO2NRDqweoUe_dAMYigjpXj9NdQJu0grZFHiroJ00wW6vb1tgt0gMaYgrTdaMFFKJZH-BucqvRbYB71_tp8vH5xeb8RXr19vLl-dlVWjHGWcrqUjaQ4zzTNWGSA4PYMq5ZxgUttcSNKBgTuRBFXQheVYVoSlFRwQrKeVVmp8nT2bcfyw7qCuzgdat6bzrtD8ppo_6MWLNTW_dVZbjICZbR4PG1gXdfRgiD6kyYetUW3BhUgQXhHOPiv6TkWErCchbJR3-Rezf6-F5HKP5KxCL04PfKl5J__lwE2Ax8My0cljjBahoLdRwLNY2FokxdvH72ajrTyXg960KU2C34X9n_qY2Ch7PA6mH0sGQ6UotpOjMmDPB9QbT_rLjIBFOf3lyqD_T9puA5V--yH-DP1so</recordid><startdate>20110406</startdate><enddate>20110406</enddate><creator>Baixauli, Francesc</creator><creator>Martín-Cófreces, Noa B</creator><creator>Morlino, Giulia</creator><creator>Carrasco, Yolanda R</creator><creator>Calabia-Linares, Carmen</creator><creator>Veiga, Esteban</creator><creator>Serrador, Juan M</creator><creator>Sánchez-Madrid, Francisco</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>Nature Publishing Group</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20110406</creationdate><title>The mitochondrial fission factor dynamin-related protein 1 modulates T-cell receptor signalling at the immune synapse</title><author>Baixauli, Francesc ; Martín-Cófreces, Noa B ; Morlino, Giulia ; Carrasco, Yolanda R ; Calabia-Linares, Carmen ; Veiga, Esteban ; Serrador, Juan M ; Sánchez-Madrid, Francisco</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5565-5db8fe4043ad1586e5e0380d53672ba80f795574779d976cc97fb7c2759266cb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Antigens</topic><topic>ATP</topic><topic>cell signalling</topic><topic>Cells</topic><topic>Docks</topic><topic>EMBO19</topic><topic>EMBO40</topic><topic>fission factor</topic><topic>Gene Silencing</topic><topic>GTP Phosphohydrolases - antagonists & inhibitors</topic><topic>GTP Phosphohydrolases - genetics</topic><topic>GTP Phosphohydrolases - metabolism</topic><topic>Humans</topic><topic>immune synapse</topic><topic>Immune system</topic><topic>Immunological Synapses - physiology</topic><topic>Immunological Synapses - ultrastructure</topic><topic>Lymphocytes - physiology</topic><topic>Microtubule-Associated Proteins - antagonists & inhibitors</topic><topic>Microtubule-Associated Proteins - genetics</topic><topic>Microtubule-Associated Proteins - metabolism</topic><topic>mitochondria</topic><topic>Mitochondria - metabolism</topic><topic>Mitochondria - ultrastructure</topic><topic>Mitochondrial Proteins - antagonists & inhibitors</topic><topic>Mitochondrial Proteins - genetics</topic><topic>Mitochondrial Proteins - metabolism</topic><topic>Mutant Proteins - genetics</topic><topic>Mutant Proteins - metabolism</topic><topic>Mutation, Missense</topic><topic>Neurons</topic><topic>Proteins</topic><topic>Receptors, Antigen, T-Cell - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Baixauli, Francesc</au><au>Martín-Cófreces, Noa B</au><au>Morlino, Giulia</au><au>Carrasco, Yolanda R</au><au>Calabia-Linares, Carmen</au><au>Veiga, Esteban</au><au>Serrador, Juan M</au><au>Sánchez-Madrid, Francisco</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The mitochondrial fission factor dynamin-related protein 1 modulates T-cell receptor signalling at the immune synapse</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2011-04-06</date><risdate>2011</risdate><volume>30</volume><issue>7</issue><spage>1238</spage><epage>1250</epage><pages>1238-1250</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>During antigen‐specific T‐cell activation, mitochondria mobilize towards the vicinity of the immune synapse. We show here that the mitochondrial fission factor dynamin‐related protein 1 (Drp1) docks at mitochondria, regulating their positioning and activity near the actin‐rich ring of the peripheral supramolecular activation cluster (pSMAC) of the immune synapse. Mitochondrial redistribution in response to T‐cell receptor engagement was abolished by Drp1 silencing, expression of the phosphomimetic mutant Drp1S637D and the Drp1‐specific inhibitor mdivi‐1. Moreover, Drp1 knockdown enhanced mitochondrial depolarization and T‐cell receptor signal strength, but decreased myosin phosphorylation, ATP production and T‐cell receptor assembly at the central supramolecular activation cluster (cSMAC). Our results indicate that Drp1‐dependent mitochondrial positioning and activity controls T‐cell activation by fuelling central supramolecular activation cluster assembly at the immune synapse.
During antigen presentation, T cells relocalize organelles, adhesion and signalling components to the immunological synapse (IS). This study shows that the localization of mitochondria to the IS is regulated by the mitochondrial fission factor Drp1 and that this is important for T‐cell activation.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>21326213</pmid><doi>10.1038/emboj.2011.25</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Antigens ATP cell signalling Cells Docks EMBO19 EMBO40 fission factor Gene Silencing GTP Phosphohydrolases - antagonists & inhibitors GTP Phosphohydrolases - genetics GTP Phosphohydrolases - metabolism Humans immune synapse Immune system Immunological Synapses - physiology Immunological Synapses - ultrastructure Lymphocytes - physiology Microtubule-Associated Proteins - antagonists & inhibitors Microtubule-Associated Proteins - genetics Microtubule-Associated Proteins - metabolism mitochondria Mitochondria - metabolism Mitochondria - ultrastructure Mitochondrial Proteins - antagonists & inhibitors Mitochondrial Proteins - genetics Mitochondrial Proteins - metabolism Mutant Proteins - genetics Mutant Proteins - metabolism Mutation, Missense Neurons Proteins Receptors, Antigen, T-Cell - metabolism T-cell receptor |
| title | The mitochondrial fission factor dynamin-related protein 1 modulates T-cell receptor signalling at the immune synapse |
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