PYK2 interacts with MyD88 and regulates MyD88-mediated NF-κB activation in macrophages

Cai Xia Xi, Fei Xiong, Zheng Zhou, Lin Mei, Wen Cheng Xiong

Research output: Contribution to journalArticle

21 Scopus citations

Abstract

PYK2, a major cell adhesion-activated tyrosine kinase, is highly expressed in macrophages and implicated in macrophage activation and inflammatory response. However, mechanisms by which PYK2 regulates inflammatory response are beginning to be understood. In this study, we demonstrate that PYK2 interacts with MyD88, a crucial signaling adaptor protein in LPS and PGN-induced NF-κB activation, in vitro and in macrophages. This interaction, increased in macrophages, stimulated by LPS, requires the death domain of MyD88. PYK2-deficient macrophages exhibit reduced phosphorylation and degradation of IκB, an inhibitor of NF-κB nuclear translocation, and decreased NF-κB activation and IL-1β expression by LPS. These results suggest that via interaction with MyD88, PYK2 is involved in modulating cytokine (e.g., LPS) stimulation of NF-κB activity and signaling, providing a mechanism underlying PYK2 regulation of an inflammatory response.

Original languageEnglish (US)
Pages (from-to)415-423
Number of pages9
JournalJournal of Leukocyte Biology
Volume87
Issue number3
DOIs
StatePublished - Mar 1 2010

Keywords

  • Integrin
  • LPS
  • Molecule
  • TLR

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Cell Biology

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