DC recognize microbial components through an array of receptors known as PRR. PRR initiate intracellular signals, which engender DC with the capacity to stimulate T-cell responses. Dectin-1 is a PRR that recognizes β-glucan, a major constituent of many fungi's outer cell wall. Here we show that Dectin-1 activates DC through phospholipase (PLC)γ2 signaling. PLCγ2-deficient DC were unable to expand antigen-specific T cells and induce TH1 and TH17 differentiation in response to β-glucan. Mechanistically, PLCγ2-deficiency impaired the capacity of DC to secrete polarizing cytokines following exposure to β-glucan. Dectin-1 required PLCγ2 to activate MAPK, AP-1 and NF-κB, which induce cytokine gene expression. Moreover, PLCγ2 controlled Dectin-1-mediated NFAT activation and induction of NFAT-dependent genes such as IL-2, cyclooxigenase-2 and Egr transcription factors.We conclude that PLCγ2 is a crucial signaling mediator that modifies DC gene expression program to activate DC responses to β-glucan-containing pathogens.

Original languageEnglish
Pages (from-to)1369-1378
Number of pages10
JournalEuropean Journal of Immunology
Issue number5
StatePublished - May 2009


  • DC
  • Dectin-1
  • PLCγ
  • Signaling


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