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- 저자 : Hyunchu Cho (검색결과 2 건)
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최의주,Eunju Kim,Hyunchu Cho,Gaeul Lee,Heawon Baek,In Young Lee 한국분자세포생물학회 2023 Molecules and cells Vol.46 No.7
Linear ubiquitin chain assembly complex (LUBAC) is a ubiquitin E3 ligase complex composed of HOIP, HOIL-1L, and SHARPIN that catalyzes the formation of linear/M1- linked ubiquitin chain. It has been shown to play a pivotal role in the nuclear factor (NF)-κB signaling induced by proinflammatory stimuli. Here, we found that tumor susceptibility gene (TSG101) physically interacts with HOIP, a catalytic component of LUBAC, and potentiates LUBAC activity. Depletion of TSG101 expression by RNA interference decreased TNFα-induced linear ubiquitination and the formation of TNFα receptor 1 signaling complex (TNFRSC). Furthermore, TSG101 facilitated the TNFα-induced stimulation of the NF-κB pathway. Thus, we suggest that TSG101 functions as a positive modulator of HOIP that mediates TNFα-induced NF-κB signaling pathway.
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MST1 Negatively Regulates TNFα-Induced NF-κB Signaling through Modulating LUBAC Activity
Lee, In Young,Lim, Jane Melissa,Cho, Hyunchu,Kim, Eunju,Kim, Yeonsil,Oh, Hye-Kyung,Yang, Woo Seok,Roh, Kyung-Hye,Park, Hyun Woo,Mo, Jung-Soon,Yoon, Je-Hyun,Song, Hyun Kyu,Choi, Eui-Ju Elsevier 2019 Molecular Cell Vol.73 No.6
<P><B>Summary</B></P> <P>The nuclear factor (NF)-κB pathway plays a central role in inflammatory and immune responses, with aberrant activation of NF-κB signaling being implicated in various human disorders. Here, we show that mammalian ste20-like kinase 1 (MST1) is a previously unrecognized component of the tumor necrosis factor α (TNFα) receptor 1 signaling complex (TNF-RSC) and attenuates TNFα-induced NF-κB signaling. Genetic ablation of MST1 in mouse embryonic fibroblasts and bone marrow-derived macrophages potentiated the TNFα-induced increase in IκB kinase (IKK) activity, as well as the expression of NF-κB target genes. TNFα induced the recruitment of MST1 to TNF-RSC and its interaction with HOIP, the catalytic component of the E3 ligase linear ubiquitin assembly complex (LUBAC). Furthermore, MST1 activated in response to TNFα stimulation mediates the phosphorylation of HOIP and thereby inhibited LUBAC-dependent linear ubiquitination of NEMO/IKKγ. Together, our findings suggest that MST1 negatively regulates TNFα-induced NF-κB signaling by targeting LUBAC.</P> <P><B>Highlights</B></P> <P> <UL> <LI> TNFα induces the recruitment of MST1 to the TNFR1 signaling complex (TNF-RSC) </LI> <LI> TRAF2 is required for the TNFα-induced activation of MST1 within the TNF-RSC </LI> <LI> MST1 phosphorylates HOIP in TNF-RSC, thereby inhibiting an E3 ligase activity of LUBAC </LI> <LI> MST1 attenuates the LUBAC-mediated activation of the NF-κB pathway </LI> </UL> </P> <P><B>Graphical Abstract</B></P> <P>[DISPLAY OMISSION]</P>
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