The mechanism of dephosphorylation of CERT by the reduction of raftcomponents

减少筏成分使CERT去磷酸化的机制

• 批准号: 20790092
• 负责人: 熊谷 圭悟
• 金额: $ 2.66万
• 依托单位: National Institute of Infectious Diseases
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Young Scientists (B)
• 财政年份: 2008
• 资助国家: 日本
• 起止时间: 2008 至 2009
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-20790092/
• 关键词: 脂質

It is known that CERT (ceramide transport protein) is activated by the dephosphorylation, which is triggered by the degradation of plasma membrane sphingomyelin or by the treatment of inhibitor for sphoingomyelin synthesis. Our research elucidated these two dephosphorylation pathway is qualitatively different. Additionally, a novel phosphorylation site of CERT was found unexpectedly, and the phosphorylation of this site had a significant effect on the previously reported multiple phosphorylation of CERT. The results suggest that the activity of CERT is regulated by more complicated, multi-step mechanism.

已知CERT（神经酰胺转运蛋白）通过去磷酸化而被激活，所述去磷酸化由质膜鞘磷脂的降解或鞘磷脂合成抑制剂的处理触发。我们的研究阐明了这两种去磷酸化途径是质的不同。此外，我们还意外地发现了CERT的一个新的磷酸化位点，该位点的磷酸化对以前报道的CERT的多重磷酸化有显著的影响。结果表明，CERT的活性受更复杂的多步骤机制的调节。

项目成果

Casein kinase Igamma2 down-regulates trafficking of ceramide in the synthesis of sphingomyelin

酪蛋白激酶 Igamma2 下调鞘磷脂合成中神经酰胺的运输

• 发表时间: 2009
• 期刊: Molecular Biology of the Cell 20
• 作者: Tomishige;N.
• 通讯作者: N.

Crystal Structures of the CERT START Domain with Inhibitors Provide Insights into the Mechanism of Ceramide Transfer

• DOI: 10.1016/j.jmb.2009.12.029
• 发表时间: 2010-02-19
• 期刊: JOURNAL OF MOLECULAR BIOLOGY
• 影响因子: 5.6
• 作者: Kudo, Norio;Kumagai, Keigo;Kato, Ryuichi
• 通讯作者: Kato, Ryuichi