T-cell death following immune activation is mediated by mitochondria-localized SARM

Cell Death Differ. 2013 Mar;20(3):478-89. doi: 10.1038/cdd.2012.144. Epub 2012 Nov 23.

Abstract

Following 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Apoptosis
  • Armadillo Domain Proteins / antagonists & inhibitors
  • Armadillo Domain Proteins / genetics
  • Armadillo Domain Proteins / metabolism*
  • Caspase 9 / metabolism
  • Cells, Cultured
  • Cytoskeletal Proteins / antagonists & inhibitors
  • Cytoskeletal Proteins / genetics
  • Cytoskeletal Proteins / metabolism*
  • Extracellular Signal-Regulated MAP Kinases / metabolism
  • HEK293 Cells
  • Humans
  • Lymphocyte Activation
  • Lymphoma, T-Cell / metabolism
  • Lymphoma, T-Cell / pathology
  • Mice
  • Mice, Transgenic
  • Mitochondria / metabolism*
  • Phosphorylation
  • Proto-Oncogene Proteins c-bcl-2 / metabolism
  • RNA Interference
  • RNA, Small Interfering / metabolism
  • T-Lymphocytes / immunology
  • T-Lymphocytes / metabolism*
  • Transfection
  • bcl-2-Associated X Protein / antagonists & inhibitors
  • bcl-2-Associated X Protein / genetics
  • bcl-2-Associated X Protein / metabolism
  • bcl-X Protein / antagonists & inhibitors
  • bcl-X Protein / genetics
  • bcl-X Protein / metabolism

Substances

  • Armadillo Domain Proteins
  • Cytoskeletal Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • RNA, Small Interfering
  • SARM1 protein, human
  • bcl-2-Associated X Protein
  • bcl-X Protein
  • Extracellular Signal-Regulated MAP Kinases
  • Caspase 9