2022 Fiscal Year Final Research Report
| Project/Area Number |
19K22514
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| Research Category |
Grant-in-Aid for Challenging Research (Exploratory)
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| Allocation Type | Multi-year Fund |
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| Review Section |
Medium-sized Section 48:Biomedical structure and function and related fields
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| Research Institution | Osaka University |
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Principal Investigator |
Harada Akihiro 大阪大学, 大学院医学系研究科, 教授 (40251441)
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| Project Period (FY) |
2019-06-28 – 2023-03-31
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| Keywords | 細胞極性 / 脱核 |
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| Outline of Final Research Achievements |
From the analysis of Rab8 and Rab8-binding proteins in various tissues, we found that the polarization mechanism of small intestinal epithelial cells has commonalities with those of erythroblasts, T cells, and renal podocytes and different from the one in renal tubules. We showed that the mechanism ``Rab8-dependent polarity mechanism'' works universally in the formation and maintenance of polarity in the above-mentioned cell types such as epithelial cells of the small intestine by the following observatons. 1.Rab8 and 10 are highly expressed in these cells. 2. Rab8 and its binding proteins co-localize to cellular recycling endosomes (RE). 3. Knockdown of these in erythroblasts decreased the enucleation efficiency.
These data were compiled and published in a paper.
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| Free Research Field |
細胞生物学
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| Academic Significance and Societal Importance of the Research Achievements |
細胞極性の形成維持機構が上皮細胞の極性のみならず、赤芽球や骨格筋の核の極性移動にも関与していることが明らかになったことで、極性には共通の分子機構があることが初めて明らかになった。これは細胞極性の分子機構の共通性を初めて示したことで学術的意義は高い。また、Rab8/10結合タンパク質EHBP1L1のノックアウトマウスやRab10のノックダウンによって赤芽球の脱核効率が低下することからEHBP1L1やRab10が脱核に重要であることが明らかとなった。この研究からEHBP1L1、Rab10のagonistが脱核効率を上げて赤血球産生を促進できる可能性が判明し社会的な意義も大きい。
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