Okamoto, Haruko - University of Southampton - Discipline of Biological Sciences

个人简介

Career history 2014-Present: Lecturer. Biological Sciences, University of Southampton, UK. 2009-2014: Assistant Professor. Faculty of Pharmaceutical Sciences, Iwate Medical University, Japan. 2008-2009: Research Associate. University of Oxford, UK. 2003-2008: BBSRC Research Fellow. University of Oxford, UK. 2001-2003: Postdoctoral Assistant. University of Oxford, UK. 1997-2001: Postdoctoral Fellow. Department of Molecular Cellular and Developmental Biology, Yale University, USA.

研究领域

G-protein signalling in plants My main interest is to dissect the molecular basis of heterotrimeric G-protein signalling in processes modulated by light. The genome of the model plant Arabidopsis encodes just one gene of each of the Gα and Gβ subunits thus providing us with a uniquely simple system. T-DNA insertion mutants as well as plants overexpressing Gα and Gβ subunit have been analysed for their physiological characteristics in response to a range of environmental signals. Our main focus is to understand the molecular basis of heterotrimeric G-protein signalling in Arabidopsis by employing techniques of molecular biology, cell biology and genetics. Light signalling pathways, mediated by a range of photoreceptors such as cryptochromes and phytochromes, have been identified as one of the many pathways in which heterotrimeric G-proteins function and therefore we are using light signals as a primary input to understand the G-protein signalling process. The role of V-ATPases: environmental sensing and medical applications The vacuole in plants and the acidic compartments such as lysosomes in animals, play a central role in cellular homeostasis and their responses to environmental stresses. The proton pump vacuolar ATPase (V-ATPase) has V1 that hydrolyses ATP and the energy is coupled to the rotation of Vo complex that forms a pore for proton transport across the membrane. However, how the V-ATPases sense and regulate proton transport activity is largely unknown. We have found several key amino acid residues in the E subunit of the V1 complex of yeast V-ATPase that are required for the regulation of activity in response to carbon availability and by temperature indicating that the V-ATPase E subunit has a role in sensing the environment. V-ATPases are implicated in both drug resistance and metastasis of cancer cells and we will use the yeast system to identify novel inhibitors of V-ATPases.

近期论文

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A chloroplast-localized protein LESION AND LAMINA BENDING affects defence and growth responses in rice - Tamiru, Muluneh, Takagi, Hiroki, Abe, Akira, Yokota, Takao, Kanzaki, Hiroyuki, Okamoto, Haruko, Saitoh, Hiromasa, Takahashi, Hideyuki, Fujisaki, Koki, Oikawa, Kaori, Uemura, Aiko, Natsume, Satoshi, Jikumaru, Yusuke, Matsuura, Hideyuki, Umemura, Kenji, Terry, Matthew J. and Terauchi, Ryohei Published:2016Publication:New PhytologistVolume:210Page Range:1282-1297doi:10.1111/nph.13864 Molecular interaction of jasmonate and phytochrome A signalling - Hsieh, Hsu-Liang and Okamoto, Haruko Published:2014Publication:Journal of Experimental BotanyPage Range:2847-2857doi:10.1093/jxb/eru230 Fern Adiantum capillus-veneris phytochrome 1 comprises two native photochemical types similar to seed plant phytochrome A - Sineshchekov, V., Koppel, L., Okamoto, H. and Wada, M. Published:2014Publication:Journal of Photochemistry and Photobiology B: BiologyVolume:130Page Range:20-29doi:10.1016/j.jphotobiol.2013.10.007PMID:24246712 Glu-44 in the amino-terminal alpha-Helix of yeast vacuolar ATPase E subunit (Vma4p) has a role for VoV1 assembly - Okamoto-Terry, Haruko, Umeki, Kaori, Nakanishi-Matsui, Mayumi and Futai, Masamitsu Published:2013Publication:Journal of Biological ChemistryVolume:288Page Range:36236-36243doi:10.1074/jbc.M113.506741 Rotational catalysis in proton pumping ATPases: From E. coli F-ATPase to mammalian V-ATPase - Futai, Masamitsu, Nakanishi-Matsui, Mayumi, Okamoto, Haruko, Sekiya, Mizuki and Nakamoto, Robert K. Published:2012Publication:Biochimica et Biophysica Acta (BBA) - BioenergeticsVolume:1817, (10)Page Range:1711-1721doi:10.1016/j.bbabio.2012.03.015PMID:22459334