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2017 ; 91
(4
): ä Nephropedia Template TP
gab.com Text
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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 PMID27903798
show 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.
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