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Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 J+Virol 2017 ; 91 (4): ä Nephropedia Template TP
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The Linear Ubiquitin Assembly Complex Modulates Latent Membrane Protein 1 Activation of NF-?B and Interferon Regulatory Factor 7 #MMPMID27903798
Wang L; Wang Y; Zhao J; Ren J; Hall KH; Moorman JP; Yao ZQ; Ning S
J Virol 2017[Feb]; 91 (4): ä PMID27903798show ga
Recently, linear ubiquitin assembly complex (LUBAC)-mediated linear ubiquitination has come into focus due to its emerging role in activation of NF-?B in different biological contexts. However, the role of LUBAC in LMP1 signaling leading to NF-?B and interferon regulatory factor 7 (IRF7) activation has not been investigated. We show here that RNF31, the key component of LUBAC, interacts with LMP1 and IRF7 in Epstein-Barr virus (EBV)-transformed cells and that LUBAC stimulates linear ubiquitination of NEMO and IRF7. Consequently, LUBAC is required for LMP1 signaling to full activation of NF-?B but inhibits LMP1-stimulated IRF7 transcriptional activity. The protein levels of RNF31 and LMP1 are correlated in EBV-transformed cells. Knockdown of RNF31 in EBV-transformed IB4 cells by RNA interference negatively regulates the expression of the genes downstream of LMP1 signaling and results in a decrease of cell proliferation. These lines of evidence indicate that LUBAC-mediated linear ubiquitination plays crucial roles in regulating LMP1 signaling and functions.IMPORTANCE We show here that LUBAC-mediated linear ubiquitination is required for LMP1 activation of NF-?B but inhibits LMP1-mediated IRF7 activation. Our findings provide novel mechanisms underlying EBV-mediated oncogenesis and may have a broad impact on IRF7-mediated immune responses.