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Chung, K.S.,Won, M.,Lee, J.J.,Ahn, J.,Hoe, K.L.,Kim, D.U.,Song, K.B.,Yoo, H.S. Elsevier Science Publishers 2007 Journal of biotechnology Vol.129 No.3
Stm1, a G-protein coupled receptor, which senses nutritional state drives cells to stop the proliferative cell cycle and enter meiosis under nutritionally deficient conditions in Schizosaccharomyces pombe. It was shown that overexpression of Stm1 led growth inhibition and uncontrolled mitotic haploidization presumably by the premature initiation of mitosis. Sty1 and Gpa2 seem to play important roles for Stm1 to deliver starvation signal to induce downstream function. Based on the observation that conversion of diploid to haploid by overexpression of Stm1 can be easily detected as pink or red colonies in the media containing low adenine, HTS drug screening system to identify modulators of GPCR was established and tested using 413 compounds. Four very potent modulators of GPCR including Biochanin A, which possess strong inhibitory activity against uncontrolled cell division, were identified in this screening. This study provides the yeast-based platform that allows robust cellular assays to identify novel modulators of G-protein signaling and MAP kinase pathway.
Jansson, K.,Warringer, J.,Farewell, A.,Park, H.O.,Hoe, K.L.,Kim, D.U.,Hayles, J.,Sunnerhagen, P. Elsevier 2008 Mutation research Vol.644 No.1
The DNA glycosylase MutY is strongly conserved in evolution, and homologs are found in most eukaryotes and prokaryotes examined. This protein is implicated in repair of oxidative DNA damage, in particular adenine mispaired opposite 7,8-dihydro-8-oxoguanine. Previous investigations in Escherichia coli, fission yeast, and mammalian cells show an association of mutations in MutY homologs with a mutator phenotype and carcinogenesis. Eukaryotic MutY homologs physically associate with several proteins with a role in replication, DNA repair, and checkpoint signaling, specifically the trimeric 9-1-1 complex. In a genetic investigation of the fission yeast MutY homolog, myh1<SUP>+</SUP>, we show that the myh1 mutation confers a moderately increased UV sensitivity alone and in combination with mutations in several DNA repair genes. The myh1 rad1, and to a lesser degree myh1 rad9, double mutants display a synthetic interaction resulting in enhanced sensitivity to DNA damaging agents and hydroxyurea. UV irradiation of myh1 rad1 double mutants results in severe chromosome segregation defects and visible DNA fragmentation, and a failure to activate the checkpoint. Additionally, myh1 rad1 double mutants exhibit morphological defects in the absence of DNA damaging agents. We also found a moderate suppression of the slow growth and UV sensitivity of rhp51 mutants by the myh1 mutation. Our results implicate fission yeast Myh1 in repair of a wider range of DNA damage than previously thought, and functionally link it to the checkpoint pathway.
Conservation and Rewiring of Functional Modules Revealed by an Epistasis Map in Fission Yeast
Roguev, A.,Bandyopadhyay, S.,Zofall, M.,Zhang, K.,Fischer, T.,Collins, S. R.,Qu, H.,Shales, M.,Park, H.-O.,Hayles, J.,Hoe, K.-L.,Kim, D.-U.,Ideker, T.,Grewal, S. I.,Weissman, J. S.,Krogan, N. J. American Association for the Advancement of Scienc 2008 Science Vol.322 No.5900
Lee, N.J.,Song, J.M.,Cho, H.J.,Sung, Y.M.,Lee, T.,Chung, A.,Hong, S.H.,Cifelli, J.L.,Rubinshtein, M.,Habib, L.K.,Capule, C.C.,Turner, R.S.,Pak, D.T.S.,Yang, J.,Hoe, H.S. Elsevier Science Publishers B.V 2016 Biochimica et biophysica acta Vol.1862 No.2
Our recent study demonstrated that an amyloid-β binding molecule, BTA-EG4, increases dendritic spine number via Ras-mediated signaling. To potentially optimize the potency of the BTA compounds, we synthesized and evaluated an amyloid-β binding analog of BTA-EG4 with increased solubility in aqueous solution, BTA-EG6. We initially examined the effects of BTA-EG6 on dendritic spine formation and found that BTA-EG6-treated primary hippocampal neurons had significantly increased dendritic spine number compared to control treatment. In addition, BTA-EG6 significantly increased the surface level of AMPA receptors. Upon investigation into the molecular mechanism by which BTA-EG6 promotes dendritic spine formation, we found that BTA-EG6 may exert its effects on spinogenesis via RasGRF1-ERK signaling, with potential involvement of other spinogenesis-related proteins such as Cdc42 and CDK5. Taken together, our data suggest that BTA-EG6 boosts spine and synapse number, which may have a beneficial effect of enhancing neuronal and synaptic function in the normal healthy brain.