The transmembrane activator TACI triggers immunoglobulin class switching by activating B cells through the adaptor MyD88

  • Bing He
  • , Raul Santamaria
  • , Weifeng Xu
  • , Montserrat Cols
  • , Kang Chen
  • , Irene Puga
  • , Meimei Shan
  • , Huabao Xiong
  • , James B. Bussel
  • , April Chiu
  • , Anne Puel
  • , Jeanine Reichenbach
  • , László Marodi
  • , Rainer Döffinger
  • , Julia Vasconcelos
  • , Andrew Issekutz
  • , Jens Krause
  • , Graham Davies
  • , Xiaoxia Li
  • , Bodo Grimbacher
  • Alessandro Plebani, Eric Meffre, Capucine Picard, Charlotte Cunningham-Rundles, Jean Laurent Casanova, Andrea Cerutti

Research output: Contribution to journalArticlepeer-review

291 Scopus citations

Abstract

BAFF and APRIL are innate immune mediators that trigger immunoglobulin G (IgG) and IgA class-switch recombination (CSR) in B cells by engaging the receptor TACI. The mechanism that underlies CSR signaling by TACI remains unknown. Here we found that the cytoplasmic domain of TACI encompasses a conserved motif that bound MyD88, an adaptor that activates transcription factor NF-κB signaling pathways via a Toll-interleukin 1 (IL-1) receptor (TIR) domain. TACI lacks a TIR domain, yet triggered CSR via the DNA-editing enzyme AID by activating NF-κB through a Toll-like receptor (TLR)-like MyD88-IRAK1-IRAK4-TRAF6-TAK1 pathway. TACI-induced CSR was impaired in mice and humans lacking MyD88 or the kinase IRAK4, which indicates that MyD88 controls a B cell-intrinsic, TIR-independent, TACI-dependent pathway for immunoglobulin diversification.

Original languageEnglish
Pages (from-to)836-845
Number of pages10
JournalNature Immunology
Volume11
Issue number9
DOIs
StatePublished - Sep 2010

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