Interleukin-1 receptor-associated kinase 2 (IRAK2)

Interleukin-1 receptor-associated kinase 2 (IRAK2) is a serine/threonine protein kinase that plays an essential role in innate immune signaling, particularly as a transducer downstream of interleukin-1 receptors (IL-1Rs) and toll-like receptors (TLRs)[3][4][5]. IRAK2 participates in NF-κB activation, mediates the stabilization and translation of cytokine and chemokine mRNAs, and is required for optimal posttranscriptional control of inflammatory gene expression following bacterial and viral challenge[1][2][4]. Structurally, IRAK2 contains an N-terminal death domain and a central kinase domain, enabling it to act as both scaffold and signaling enzyme[2]. It interacts with key partners such as TRAF6 and MyD88, and is crucial for sustaining immune responses during prolonged pathogen sensing[2][3][4]. Genetic variation or disruption of IRAK2 impairs inflammation and confers resistance to endotoxic shock at the cost of diminished cytokine output, making it a potential therapeutic target in diseases driven by excessive innate immune activation[1][2][5].

Other names

Interleukin-1 receptor-associated kinase-like 2IRAK-2Pelle-like protein kinase

Inhibitors would block IRAK2 kinase activity, reducing downstream NF-κB activation and inflammatory cytokine production