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- 저자 : Jane Melissa Lim (검색결과 2 건)
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이라나,Jane Melissa Lim,노경혜,김지현,강성만,이지은,최의주 한국통합생물학회 2016 Animal cells and systems Vol.20 No.6
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease with the selective loss of motor neurons in the brain, brain stem, and spinal cord. A number of the mutants of the human gene for superoxide dismutase 1 (SOD1) have been shown to cause familial ALS as a result of gain-offunction toxicity by an unknown mechanism. In this study, we show that glyceraldehyde-3- phosphate dehydrogenase (GAPDH) functions as a critical mediator of the apoptotic cell death signaling cascade induced by the ALS-associated G93A mutant of human SOD1 [SOD1(G93A)]. We observed that SOD1(G93A) induces S-nitrosylation of GAPDH and the subsequent binding of GAPDH and Siah1 in NSC34 motor neuron-like cells. Furthermore, SOD1(G93A) promoted nuclear translocation of S-nitrosylated GAPDH in the cells. In addition, SOD1(G93A)-induced apoptotic cell death was inhibited by deprenyl, a chemical inhibitor of GAPDH S-nitrosylation, in NSC34 cells. Taken together, our findings suggest that S-nitrosylation of GAPDH plays a critical role in SOD1(G93A)-induced neuronal apoptosis.
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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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