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This study for the first time ever reports the association of IRAK2 rs3844283, IRAK2 rs708035, and the corresponding haplotypes with rheumatoid arthritis.
IRAK2 L392V showed intact binding to, but impaired ubiquitination of, tumor necrosis factor receptor-associated factor 6, a vital step in signal transduction
This for the first time implicates human IRAK2 in a human disease and highlights the R214G IRAK2 variant as a potential novel and broadly applicable biomarker for disease or as a therapeutic intervention point.
Human miR-373 is silenced by histone modification in lung cancer cells and is a negative regulator of the mesenchymal phenotype through downstream IRAK2 and LAMP1 target genes.
Results suggest that D431E-IRAK2 (interleukin-1 receptor-associated kinase-2) increases NF-kappaB activation by promoting TRAF6 ubiquitination by enhancing TNF Receptor-Associated Factor 6 (TRAF6)-IRAK2 interaction.
These findings demonstrate an unexpected linkage of the innate immunity machinery to unfolded protein response signaling, revealing IRAK2 as a novel amplifier of the IRE1 pathway.
Human interleukin-1 receptor-associated kinase-2 is essential for Toll-like receptor-mediated transcriptional and post-transcriptional regulation of tumor necrosis factor alpha.
analysis of differential regulation of interleukin-1 receptor-associated kinase-1 (IRAK-1) and IRAK-2 by microRNA-146a and NF-kappaB in stressed human astroglial cells and in Alzheimer disease
Our data show that interleukin-1R-associated kinase 2 is a novel and critical component of TGFbeta signaling.
the crystal structure of the MyD88-IRAK4-IRAK2 death domain (DD) complex, which surprisingly reveals a left-handed helical oligomer that consists of 6 MyD88, 4 IRAK4 and 4 IRAK2 DDs
CTCF plays a major role in IRAK2 transcription; EMSA revealed a CTCF-binding site within the mouse Irak2 promoter
IRAK-2 plays a more central role than IRAK-1 in TLR signaling to NFkappaB through TRAF6 ubiquitination
TRAF6 and interleukin receptor-associated kinase 2 are novel binding partners for PS1, and IL-1R1 is a new substrate for presenilin-dependent gamma-secretase cleavage
In summary, lipopolysaccharide activates a nuclear function of IRAK2 that facilitates the assembly of nuclear export machinery to export selected inflammatory mRNAs to the cytoplasm for translation.
Our results establish that the IRAK2-TRAF6 interaction is rate limiting for the late, but not the early phase of cytokine production in bone marrow-derived macrophages and plasmacytoid dendritic cells
IRAK2 plays a key role in the TLR9-mediated transcriptional regulation of Irak-m expression by sustaining activation of PKD1 and NF-kappaB
IRAK-2 mediates pathology in a CD4 T cell specific manner by promoting Th17 cell development through enhancement of IL-1beta-induced activation of transcription factors RORgammat and BATF.
the kinase activity of IRAK2 is required for the optimal activation of mitogen-activated protein kinase signaling, which regulates cytokine and chemokine production at posttranscriptional levels.
IRAK2 is a negative regulator of Toll-like receptor (TLR)9-induced interferon production in plasmacytoid dendritic cells.
Alternative splicing of the Irak2 gene in mice will generate agonistic or antagonistic Irak2 isoforms, which is likely to have consequences for the regulation of Toll-like receptors signaling.
These results reveal that IRAK2 is required for LPS-mediated post-transcriptional control of cytokine and chemokine expression, which plays an essential role in TLR4-induced septic shock.
Data demonstrate that IRAK-2 is an essential component of the early TLR response in MOLF/Ei mice and show a distinct pathway of p38 and NF-kappaB activation in this model organism.
miR-146a, up-regulated during viral infection, is a negative regulator of the RIG-I-dependent antiviral pathway by targeting TRAF6, IRAK1, and IRAK2.
IRAK2 encodes the interleukin-1 receptor-associated kinase 2, one of two putative serine/threonine kinases that become associated with the interleukin-1 receptor (IL1R) upon stimulation. IRAK2 is reported to participate in the IL1-induced upregulation of NF-kappaB.
interleukin-1 receptor associated kinase-2
, interleukin-1 receptor-associated kinase-like 2
, interleukin-1 receptor-associated kinase 2c