| c-Cbl介导了hSef的泛素化和降解 |
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| 引用本文： | 任永明,荣知立,李智勇,程龙,李颖华,王银银,任芳丽,David M.Irwin,常智杰.c-Cbl介导了hSef的泛素化和降解[J].生物化学与生物物理进展,2008,35(1):43-49. |
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| 作者姓名： | 任永明 荣知立 李智勇 程龙 李颖华 王银银 任芳丽 David M.Irwin 常智杰 |
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| 作者单位： | 1. 清华大学医学院,清华大学生物科学与技术系,生物膜与膜生物技术国家重点实验室,北京,100084
2. Department of Laboratory Medicine and Pathobiology;University of Toronto,Toronto,Ont,Canada |
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| 基金项目： | 清华大学 985 项目, 清华大学-裕元医学基金资助项目, 国家自然科学基金 (30530420, 30470888，30470703), 国家重点基础研究发展计划(973)(2001CB510006, 2002CB513007, 2006CB910100)和北京市科学研究基金(H020220020310)资助项目. |
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| 摘 要： | Sef(similar expression to fgf genes)作为FGF信号通路中可诱导的拮抗分子相继在斑马鱼,小鼠,和人类中被鉴定出来,并进行了相应的功能研究.目前对于Sef蛋白本身稳定性的研究还未见报道.对c-Cbl对Sef稳定性的影响进行了研究.免疫荧光实验表明Sef能够和c-Cbl蛋白在细胞中发生共定位,随后的免疫共沉淀实验证明Sef能够和c-Cbl发生相互作用.体内泛素化实验表明c-Cbl能够使Sef发生明显的泛素化作用.这种泛素化最终导致了Sef本身的剂量依赖性的降解.针对c-Cbl的siRNA表达也使Sef稳定细胞系的表达水平得到恢复.结果表明,c-Cbl对Sef的泛素化及降解可能作为一种调控拮抗因子的蛋白质水平从而最终调节信号通路的一种机制.
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| 关 键 词： | hSef c-Cbl 泛素化 降解 hSef c-Cbl ubiquitination degradation 泛素化 降解 Degradation serve modulator protein stability during signal transduction Data interaction protein degradation Results possible role however regulation remains function different ways mouse |
| 收稿时间： | 2007-04-13 |
| 修稿时间： | 2007-05-30 |
c-Cbl Mediated Ubiquitination and Degradation of hSef |
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| REN Yong-Ming,RONG Zhi-Li,LI Zhi-Yong,CHENG Long,LI Ying-Hu,WANG Yin-Yin,REN Fang-Li,David M.Irwin and CHANG Zhi-Jie.c-Cbl Mediated Ubiquitination and Degradation of hSef[J].Progress In Biochemistry and Biophysics,2008,35(1):43-49. |
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| Authors: | REN Yong-Ming RONG Zhi-Li LI Zhi-Yong CHENG Long LI Ying-Hu WANG Yin-Yin REN Fang-Li David MIrwin and CHANG Zhi-Jie |
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| Institution: | School of Medicine, Department of Biological Sciences and Biotechnology, State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua University, Beijing 100084, China;School of Medicine, Department of Biological Sciences and Biotechnology, State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua University, Beijing 100084, China;School of Medicine, Department of Biological Sciences and Biotechnology, State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua University, Beijing 100084, China;School of Medicine, Department of Biological Sciences and Biotechnology, State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua University, Beijing 100084, China;School of Medicine, Department of Biological Sciences and Biotechnology, State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua University, Beijing 100084, China;School of Medicine, Department of Biological Sciences and Biotechnology, State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua University, Beijing 100084, China;School of Medicine, Department of Biological Sciences and Biotechnology, State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua University, Beijing 100084, China;Department of Laboratory Medicine and Pathobiology; University of Toronto, Toronto, Ont, Canada;School of Medicine, Department of Biological Sciences and Biotechnology, State Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua University, Beijing 100084, China |
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| Abstract: | Sef (similar expression to fgf genes) was identified as a feedback antagonist of FGF signaling in zerbrafish, mouse and human. Sef has been reported to function in different ways, however the regulation of Sef stability remains unknown. The possible role of c-Cbl in the regulation of Sef protein degradation was investigated. Results from coimmunoprecipitation and immunostaining assays reveal that hSef colocalizes and interacts with c-Cbl. Data suggest that the interaction between hSef and c-Cbl results in the ubiquitination and subsequent degradation of the hSef protein. It was proposed that c-Cbl may serve as a modulator to regulate Sef protein stability during FGF signal transduction. |
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| Keywords: | hSef c-Cbl ubiquitination degradation |
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