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dc.contributor.authorPanneerselvam, P.
dc.contributor.authorSingh, L. P.
dc.contributor.authorSelvarajan, V.
dc.contributor.authorChng, W. J.
dc.contributor.authorNg, S. B.
dc.contributor.authorTan, N. S.
dc.contributor.authorHo, B.
dc.contributor.authorDing, Jeak Ling
dc.contributor.authorChen, Jianzhu
dc.date.accessioned2014-01-21T17:51:46Z
dc.date.available2014-01-21T17:51:46Z
dc.date.issued2012-11
dc.date.submitted2012-09
dc.identifier.issn1350-9047
dc.identifier.issn1476-5403
dc.identifier.urihttp://hdl.handle.net/1721.1/84108
dc.description.abstractFollowing acute-phase infection, activated T cells are terminated to achieve immune homeostasis, failure of which results in lymphoproliferative and autoimmune diseases. We report that sterile α- and heat armadillo-motif-containing protein (SARM), the most conserved Toll-like receptors adaptor, is proapoptotic during T-cell immune response. SARM expression is significantly reduced in natural killer (NK)/T lymphoma patients compared with healthy individuals, suggesting that decreased SARM supports NK/T-cell proliferation. T cells knocked down of SARM survived and proliferated more significantly compared with wild-type T cells following influenza infection in vivo. During activation of cytotoxic T cells, the SARM level fell before rising, correlating inversely with cell proliferation and subsequent T-cell clearance. SARM knockdown rescued T cells from both activation- and neglect-induced cell deaths. The mitochondria-localized SARM triggers intrinsic apoptosis by generating reactive oxygen species and depolarizing the mitochondrial potential. The proapoptotic function is attributable to the C-terminal sterile alpha motif and Toll/interleukin-1 receptor domains. Mechanistically, SARM mediates intrinsic apoptosis via B cell lymphoma-2 (Bcl-2) family members. SARM suppresses B cell lymphoma-extra large (Bcl-xL) and downregulates extracellular signal-regulated kinase phosphorylation, which are cell survival effectors. Overexpression of Bcl-xL and double knockout of Bcl-2 associated X protein and Bcl-2 homologous antagonist killer substantially reduced SARM-induced apoptosis. Collectively, we have shown how T-cell death following infection is mediated by SARM-induced intrinsic apoptosis, which is crucial for T-cell homeostasis.en_US
dc.description.sponsorshipSingapore-MIT Alliance Computational and Systems Biology Flagship Projecten_US
dc.language.isoen_US
dc.publisherNature Publishing Groupen_US
dc.relation.isversionofhttp://dx.doi.org/10.1038/cdd.2012.144en_US
dc.rightsCreative Commons Attribution-NonCommercial-No Derivative Works 3.0 Unported Licenseen_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/en_US
dc.sourceCell Death and Differentiationen_US
dc.titleT-cell death following immune activation is mediated by mitochondria-localized SARMen_US
dc.typeArticleen_US
dc.identifier.citationPanneerselvam, P, L P Singh, V Selvarajan, W J Chng, S B Ng, N S Tan, B Ho, J Chen, and J L Ding. “T-cell death following immune activation is mediated by mitochondria-localized SARM.” Cell Death and Differentiation 20, no. 3 (November 23, 2012): 478-489. © 2014 ADMC Associazione Differenziamento e Morte Cellulareen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biologyen_US
dc.contributor.departmentKoch Institute for Integrative Cancer Research at MITen_US
dc.contributor.mitauthorChen, Jianzhuen_US
dc.relation.journalCell Death and Differentiationen_US
dc.eprint.versionFinal published versionen_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsPanneerselvam, P; Singh, L P; Selvarajan, V; Chng, W J; Ng, S B; Tan, N S; Ho, B; Chen, J; Ding, J Len_US
dc.identifier.orcidhttps://orcid.org/0000-0002-5687-6154
mit.licensePUBLISHER_CCen_US
mit.metadata.statusComplete


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