Our results show that CARM1 directly binds to the NF‐κB subunit p65 and synergistically coactivates NF‐κB‐mediated transactivation, in concert with the transcriptional coactivators p300/CBP and the p160 family of steroid receptor coactivators.

Carm1 knockout cells showed impaired expression of a subset of NF-κB-dependent genes upon TNFα or LPS stimulation. CARM1 forms a complex with p300 and NF-κB in vivo and interacts directly with the NF-κB subunit p65 in vitro. CARM1 seems to act in a gene-specific manner mainly by enhancing NF-κB recruitment to cognate sites.

2006年7月1日 · Chromatin immunoprecipitation demonstrated CARM1 recruitment in vivo to the promoters of NF-κB p65-regulated genes along with CBP and steroid receptor coactivator-1. This was accompanied by an increase in histone H3-R17 methylation as well as H3-K9 and H3-K14 acetylation, and a decrease in H3-citrulline.

2008年3月28日 · Our results show that PRMT1 directly binds to the NF-κB subunit p65 and synergistically coactivates NF-κB-dependent gene expression at the CARM1-dependent macrophage inflammatory protein 2 (MIP2) 16 and human immunodeficiency virus 1 (HIV-1) long terminal repeat (LTR) promoters in concert with the …

Chromatin immunoprecipitation demonstrated CARM1 recruitment in vivo to the promoters of NF-kappaB p65-regulated genes along with CBP and steroid receptor coactivator-1. This was accompanied by an increase in histone H3-R17 methylation as well as H3-K9 and H3-K14 acetylation, and a decrease in H3-citrulline.

最初发现CARM1和核受体辅助因子p160结合调控生物学功能 [4]。后来研究发现CARM1与转录因子cAMP反应元件结合蛋白CBP、β-catenin和NF-κB的p65结合调控下游靶基因的转录 [5] [6] [7]。很多研究表明CARM1在肿瘤的发生、发展和转移过程发挥着重要作用。

A total of 25 ng protein per sample was loaded on 10% SDS-protein gels and analyzed by Western blotting with anti-CARM1, anti-p65, and antiactin antibodies.

Western blot结果显示，在IL-1β诱导/OE CARM1时，促进P65磷酸化为PP65,加入CARM1 inhibitor后，上述情况得到缓解。 共定位结果显示:IL-1β诱导下，P65磷酸化增加，加入CARM1 inhibitor后，上述情况得到缓解。

2005年1月12日 · Carm1 knockout cells showed impaired expression of a subset of NF-kappaB-dependent genes upon TNFalpha or LPS stimulation. CARM1 forms a complex with p300 and NF-kappaB in vivo and interacts directly with the NF-kappaB subunit p65 in vitro.

Instead, it seems that CARM1 regulates NF-κB-mediated gene expression through complex formations with p65 and p300. Consequently, CARM1 acts as a primary coactivator by enhancing NF-κB recruitment to cognate sites and by controlling transcription in a gene-specific manner .