c-Cbl Mediated Ubiquitination and Degradation of hSef
- VernacularTitle:c-Cbl介导了hSef的泛素化和降解
- Author:
Yongming REN
;
Zhili RONG
;
Zhiyong LI
;
Long CHENG
;
Yinghua LI
;
Yinyin WANG
;
Fangli REN
;
M.irwin DAVID
;
Zhijie CHANG
- Publication Type:Journal Article
- Keywords:
hSef;
c-Cbl;
ubiquitination;
degradation
- From:
Progress in Biochemistry and Biophysics
2008;35(1):43-49
- CountryChina
- Language:Chinese
-
Abstract:
Sef (similar expression to fgf genes) was identified as a feedback antagonist of FGF signaling in zerbrafish, mouse and human. Sefhas 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.
