• Reproductive and Developmental Biology
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• v.38 no.1
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• pp.41-52
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• 2014

Embryonic genome activation (EGA) is a highly complex phenomenon that is controlled at various levels. New studies have ascertained some molecular mechanisms that control EGA in several species; it is apparent that these same mechanisms regulate EGA in all species. Protein phosphorylation, DNA methylation and histone modification regulate transcriptional activities, and mechanisms such as ubiquitination, SUMOylation and microRNAs post-transcriptionally regulate development. Each of these regulations is highly dynamic in the early embryo. A better understanding of these regulatory strategies can provide the possibility to improve the reproductive properties in mammals such as pigs, to develop methods of generating high-quality embryos in vitro, and to find markers for selecting developmentally competent embryos.

• Journal of Microbiology and Biotechnology
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• v.27 no.3
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• pp.610-615
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• 2017

When Shigella infect host cells, various effecter molecules are delivered into the cytoplasm of the host cell through the type III secretion system (TTSS) to facilitate their invasion process and control the host immune responses. Among these effectors, the S. flexneri effector OspF dephosphorylates mitogen-activated protein kinases and translocates itself to the nucleus, thus preventing histone H3 modification to regulate expression of proinflammatory cytokines. Despite the critical role of OspF, the mechanism by which it localizes in the nucleus has remained to be elucidated. In the present study, we identified a potential small ubiquitin-related modifier (SUMO) modification site within OspF and we demonstrated that Shigella TTSS effector OspF is conjugated with SUMO in the host cell and this modification mediates the nuclear translocation of OspF. Our results show a bacterial virulence factor can exploit host post-translational machinery to execute its intracellular trafficking.

• BMB Reports
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• v.42 no.1
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• pp.22-27
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• 2009

Replication Protein A (RPA) is a single stranded DNA-binding protein involved in DNA metabolic activities such as replication, repair, and recombination. RPA-Interacting Protein $\alpha$ ($RIP{\alpha}$) was originally identified as a nuclear transporter of RPA in Xenopus. The human $RIP{\alpha}$ gene encodes several splice isoforms, of which $hRIP{\alpha}$ and $hRIP{\beta}$ are the major translation products in vivo. However, limited information is available about the alternative splicing of $RIP{\alpha}$ in eukaryotes, apart from that in humans. In this study, we examined the alternative splicing of RIP{\alpha} in the Drosophila, Xenopus, and mouse system. We showed that the number of splice isoforms of RIP{\alpha} was species-specific, and displayed a tendency to increase in higher eukaryotes. Moreover, a mouse ortholog of $hRIP{\alpha}$, $mRIP{\beta}2$, was not SUMOylated, in contrast to $hRIP{\alpha}$. Based on these results, we suggest that the $RIP{\alpha}$ gene gains more splice isoforms and additional modifications after molecular evolution.

• BMB Reports
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• v.47 no.4
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• pp.233-238
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• 2014

Polypyrimidine tract-binding protein 1 (PTBP1) and its brain-specific homologue, PTBP2, are associated with pre-mRNAs and influence pre-mRNA processing, as well as mRNA metabolism and transport. They play important roles in neural differentiation and glioma development. In our study, we detected the expression of the two proteins in glioma cells and predicted that they may be sumoylated using SUMOplot analyses. We confirmed that PTBP1 and PTBP2 can be modified by SUMO1 with co-immunoprecipitation experiments using 293ET cells transiently co-expressing SUMO1 and either PTBP1 or PTBP2. We also found that SUMO1 modification of PTBP2 was enhanced by Ubc9 (E2). The mutation of the sumoylation site (Lys137) of PTBP2 markedly inhibited its modification by SUMO1. Interestingly, in T98G glioma cells, the level of sumoylated PTBP2 was reduced compared to that of normal brain cells. Overall, this study shows that PTBP2 is posttranslationally modified by SUMO1.

• KSBB Journal
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• v.24 no.3
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• pp.217-226
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• 2009

p53 undergoes various post-translational modifications, including phosphorylation, ubiquitination, sumoylation, acetylation, methylation, and poly(ADP-ribosyl)ation. Modification of p53 widely affects to various functions of p53. Acetylation and phosphorylation of p53 have been studied for regulating its transcriptional activity which is observed in various stress condition. Otherwise, ubiquitination of p53 by Mdm2 has been well-studied as a canonical ubiquitin-mediated proteasomal degradation pathway. Moreover several investigators have recently reported that ubiquitination of p53 modulates not only its proteasome-dependent degradation by poly-ubiquitination but also its localization and transcriptional activity by mono-ubiquitination which usually does not serve the proteasome dependent degradation. Here we review recent studies on the cellular functions of p53 regulated by post-translational modifications, particularly focusing on mechanisms of ubiquitination.