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Post-translational control of NF-jB signaling by ubiquitination
원민호,Hee Sun Byun,박경아,허강민 대한약학회 2016 Archives of Pharmacal Research Vol.39 No.8
The transcription factor nuclear factor-kappa B(NF-jB) controls a number of essential cellular functions,including the immune response, cell proliferation, andapoptosis. NF-jB signaling must be engaged temporallyand spatially and well orchestrated to prevent aberrantactivation because loss of normal regulation of NF-jB is amajor contributor to a variety of pathological diseases,including inflammatory diseases, autoimmune diseases,and cancers. Thus, understanding the molecular mechanismscontrolling NF-jB activation is an important part oftreatment of these relevant diseases. Although NF-jBtranscriptional activity is largely regulated by nucleartranslocation, post-translational modification of NF-jBsignaling components, including phosphorylation, ubiquitination,acetylation, and methylation, has emerged as animportant mechanism affecting activity. Many proteinshave been shown to ubiquitinate and regulate NF-jBactivation at the receptor signaling complex in response toa variety of ligands, such as tumor necrosis factor, interleukin-1, and Toll-like receptor ligands. In this review, wediscuss our current knowledge of ubiquitination patternsand their functional role in NF-jB regulation.
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Prevention of TNF-induced necrotic cell death by rottlerinthrough a Nox1 NADPH oxidase
변희선,원민호,박경아,김영래,Byung Lyul Choi,Hyunji Lee,Jang Hee Hong,Longzhen Piao,박종선,김진만,Gi Ryang Kweon,Sung Hyun Kang,한진,허강민 생화학분자생물학회 2008 Experimental and molecular medicine Vol.40 No.2
Previous studies have demonstrated that rottlerin, a specific PKCδ inhibitor, potentiates death receptor- mediated apoptosis through a cytochrome c-depend-ent or -independent pathway. However, its ability to regulate necrotic cell death, as well as the underlying ine fibrosarcoma L929 cells, treatment with rotlerin protected the cells against TNF-induced necrosis, whereas it sensitized the cels to apoptosis induced by co-treatment with Hsp90 inhibitor geldanamycin and TNF, in a maner independent of its ability to inhibit PKC-δ. TNF treatment induced rapid accumulation of mitochondrial superoxide (O2-) through the Nox1 NADPH oxidase when cells undergo necrosis. More-GTP-bound form of small GTPase Rac1 by TNF treat-ment, and subsequently suppressed mitochondrial O2- production and poly(ADP-ribose) polymerase activa-tion, thus inhibiting necrotic cell death. Therefore, our study suggests that Nox1 NADPH oxidase is a new mo-lecular target for anti-necrotic activity of rotlerin upon death-receptor ligation.
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Siah Ubiquitin Ligases Modulate Nodal Signaling during Zebrafish Embryonic Development
강나미,원민호,이명철,노현주 한국분자세포생물학회 2014 Molecules and cells Vol.37 No.5
Siah2 is a zebrafish homologue of mammalian Siah family. Siah acts as an E3 ubiquitin ligase that binds proteins destined for degradation. Extensive homology between siah and Drosophila Siah homologue (sina) suggests their important physiological roles during embryonic development. However, detailed functional studies of Siah in vertebrate development have not been carried out. Here we report that Siah2 specifically augments nodal related gene expression in marginal blastomeres at late blastula through early gastrula stages of zebrafish embryos. Siah2 dependent Nodal signaling augmentation is confirmed by cell-based reporter gene assays using 293T cells and 3TP-luciferase reporter plasmid. We also established a molecular hierarchy of Siah as a upstream regulator of FoxH1/Fast1 transcriptional factor in Nodal signaling. Elevated expression of nodal related genes by overexpre-ssion of Siah2 was enough to override the inhibitory effects of atv and lft2 on the Nodal signaling. In particular, E3 ubiquitin ligase activity of Siah2 is critical to limit the duration and/or magnitude of Nodal signaling. Additionally, since the embryos injected with Siah morpholinos mimicked the atv overexpression phenotype at least in part, our data support a model in which Siah is involved in mesendoderm patterning via modulating Nodal signaling.
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석정호,박경아,변희선,원민호,신상희,최병렬,이현지,김영래,홍장희,박종선,허강민 대한약리학회 2008 The Korean Journal of Physiology & Pharmacology Vol.12 No.4
Activation of c-Jun N-terminal kinase (JNK), a member of the mitogen-activated protein kinase family, is an important cellular response that modulates the outcome of the cells which are exposed to the tumor necrosis factor (TNF) or the genotoxic stress including DNA damaging agents. Although it is known that JNK is activated in response to genotoxic stress, neither the pathways to transduce signals to activate JNK nor the primary sensors of the cells that trigger the stress response have been identified. Here, we report that the receptor interacting protein (RIP), a key adaptor protein of TNF signaling, was required to activate JNK in the cells treated with certain DNA damaging agents such as adriamycin (Adr) and 1-β-D-arabinofuranosylcytosine (Ara-C) that cause slow and sustained activation, but it was not required when treated with N-methyl-N-nitro-N-nitrosoguanidine (MNNG) and short wavelength UV, which causes quick and transient activation. Our findings revealed that this sustained JNK activation was not mediated by the TNF (tumor necrosis factor) receptor signaling, but it required a functional ATM (ataxia telangiectasia) activity. In addition, JNK inhibitor SP-600125 significantly blocked the Adr-induced cell death, but it did not affect the cell death induced by MNNG. These findings suggest that the sustained activation of JNK mediated by RIP plays an important role in the DNA damage-induced cell death, and that the duration of JNK activation relays a different stress response to determine the cell fate.
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Kee K. Kim,Yong-Eun Kim,Jong Ok Kim,Ki-Sun Park,원민호,Kyoon Eon Kim 한국분자세포생물학회 2016 Molecules and cells Vol.39 No.8
The RNA-binding protein Rbfox3 is a well-known splicing regulator that is used as a marker for post-mitotic neurons in various vertebrate species. Although recent studies indicate a variable expression of Rbfox3 in non-neuronal tissues, including lung tissue, its cellular function in lung cancer remains largely unknown. Here, we report that the number of RBFOX3-positive cells in tumorous lung tissue is lower than that in normal lung tissue. As the transforming growth factor- (TGF-) signaling pathway is important in cancer progression, we investigated its role in RBFOX3 expression in A549 lung adenocarcinoma cells. TGF-1 treatment inhibited RBFOX3 expression at the transcriptional level. Further, RBFOX3 depletion led to a change in the expression levels of a subset of proteins related to epithelial-mesenchymal transition (EMT), such as E-cadherin and Claudin-1, during TGF-1-induced EMT. In immunofluorescence microscopic analysis, mesenchymal morphology was more prominent in RBFOX3-depleted cells than in control cells. These findings show that TGF--induced RBFOX3 inhibition plays an important role in EMT and propose a novel role for RBFOX3 in cancer progression.
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