Analysis of the regulatory mechanism of Lamin A degradation by RFP and its significance in malignant transformation.

RFP降解Lamin A的调控机制及其在恶性转化中的意义分析

• 批准号: 21890097
• 负责人: KATO Takuya
• 金额: $ 1.7万
• 依托单位: Nagoya University
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Research Activity Start-up
• 财政年份: 2009
• 资助国家: 日本
• 起止时间: 2009 至 2010
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/en/grant/KAKENHI-PROJECT-21890097/
• 关键词: Lamin A; RFP; Ubiquitin; 蛋白分解

We found that Ret Finger Protein (RFP) catalyze the ubiquitination of Lamin A. We could not prove the degradation of Lamin A by ubiquitination as initially envisioned, however, we found that both RFP and Lamin A can positively regulate cancer cell migration. Therefore, our findings indicate another possibility that RFP regulates the Lamin A's function through its ubiquitination. Since there is no report that the mechanism regulates Lamin A through ubiquitination, our results preface the novel investigation of regulation of Lamin A.

我们发现Ret Finger Protein（RFP）催化核纤层蛋白A的泛素化。我们不能证明如最初设想的那样通过泛素化降解核纤层蛋白A，然而，我们发现RFP和核纤层蛋白A都可以正向调节癌细胞迁移。因此，我们的研究结果表明另一种可能性，RFP调节核纤层蛋白A的功能，通过其泛素化。由于还没有报道通过泛素化调控核纤层蛋白A，我们的研究结果为核纤层蛋白A调控的新研究奠定了基础。

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