| Project/Area Number |
11680701
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Cell biology
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| Research Institution | Hiroshima University |
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Principal Investigator |
HIRATA Dai Hiroshima University, Graduate School Associate of Advanced Sciences Professor of Matter, 大学院・先端物質科学研究科, 助教授 (30243603)
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| Project Period (FY) |
1999 – 2000
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| Project Status |
Completed (Fiscal Year 2000)
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| Budget Amount *help |
¥3,800,000 (Direct Cost: ¥3,800,000)
Fiscal Year 2000: ¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 1999: ¥2,200,000 (Direct Cost: ¥2,200,000)
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| Keywords | Morphogenesis / Cell cycle / Yeast / Checkpoint / 成長極性 |
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| Research Abstract |
Cell morphogenesis is closely regulated with cell proliferation. I studied the checkpoint mechanism of this coordination using budding and fission yeasts.
1. Fission yeast α-glucan synthase Mok1 requires the actin cytoskeleton to localize the sites of growth and plays an essential role in cell morphogenesis downstream of protein kinase C function : We have isolated mok1^+ in a genetic screen to identify downstream effectors for Pck1/2. Mok1 has α-glucan synthase activity and plays a crucial role in cell morphogenesis.
2. Functional dissection and hierarchy of tubulin-folding cofactor homologues in fission yeast : We identified fission yeast homologues of tubulin-folding cofactors B (Alp11) and E (Alp21).
3. Overproduction of elongation factor 1α, an essential translational component, causes aberrant cell morphology by affecting the control of growth polarity in fission yeast : We showed that fission yeast EF1α has the ability to alter the morphology of yeast by affecting the control of actin and microtubule cytoskeletons.
4. A positive screening for drugs that specifically inhibit the Ca^<2+>-signaling activity on the basis of the growth-promoting effect on a yeast mutant with a peculiar phenotype : We developed a novel drug screening procedure designed to detect the active compounds that inhibit the Ca^<2+>-signaling pathway.
5. Regulation of Weel kinase in response to protein synthesis inhibition : Weel was essential for the G2 delay upon a partial inhibition of protein synthesis. Indeed, the protein synthesis inhibition caused an increase in the Weel protein by the Sty1 MAPK-dependent transcriptional and the Sty1 MAPK-independent post-transcriptional regulations.
6. GSK-3 kinase Mck1 and calcineurin coordinately mediate Hsl1 down-regulation by Ca^<2+> in budding yeast : We identified Mck1 kinase, as a component of the Ca^<2+>-signaling pathway. Mck1 functions downstream of the Mpk1 pathway and down-regulate Hsl1 kinase.
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