Role of Ca2(+)/Calmodulin-Dependent Kinase II-IRAK1 Interaction in LMP1-Induced NF-kappa B Activation
- Authors
- Kim, Jung-Eun; Kim, Sang Yong; Lim, Sue Yeon; Kieff, Elliott; Song, Yoon-Jae
- Issue Date
- Feb-2014
- Publisher
- AMER SOC MICROBIOLOGY
- Citation
- MOLECULAR AND CELLULAR BIOLOGY, v.34, no.3, pp.325 - 334
- Journal Title
- MOLECULAR AND CELLULAR BIOLOGY
- Volume
- 34
- Number
- 3
- Start Page
- 325
- End Page
- 334
- URI
- https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/12867
- DOI
- 10.1128/MCB.00912-13
- ISSN
- 0270-7306
- Abstract
- We have previously reported that interleukin-1 (IL-1) receptor-associated kinase (IRAK1) is essential for Epstein-Barr virus (EBV) latent infection membrane protein 1 (LMP1)-induced p65/RelA serine 536 phosphorylation and NF-kappa B activation but not for I kappa B kinase alpha (IKK alpha) or IKK beta activation (Y. J. Song, K. Y. Jen, V. Soni, E. Kieff, and E. Cahir-McFarland, Proc. Natl. Acad. Sci. U.S.A. 103: 2689-2694, 2006, doi: 10.1073/pnas.0511096103). Since the kinase activity of IRAK1 is not required for LMP1-induced NF-kappa B activation, IRAK1 is proposed to function as a scaffold protein to recruit a p65/RelA serine 536 kinase(s) to enhance NF-kappa B-dependent transcriptional activity. We now report that Ca2+/calmodulin-dependent protein kinase II (CaMKII) interacts with IRAK1 and is critical for LMP1-induced p65/RelA serine 536 phosphorylation and NF-kappa B activation. CaMKII bound the death domain of IRAK1 and directly phosphorylated p65/RelA at serine 536 in vitro. Downregulation of CaMKII activity or expression significantly reduced LMP1-induced p65/RelA serine 536 phosphorylation and NF-kappa B activation. Furthermore, LMP1-induced CaMKII activation and p65/RelA serine 536 phosphorylation were significantly reduced in IRAK1 knockout (KO) mouse embryonic fibroblasts (MEFs). Thus, IRAK1 may recruit and activate CaMKII, which phosphorylates p65/RelA serine 536 to enhance the transactivation potential of NF-kappa B in LMP1-induced NF-kappa B activation pathway.
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