کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1932980 | 1050599 | 2010 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Anaphase-promoting complex/cyclosome-cdh1 mediates the ubiquitination and degradation of TRB3 Anaphase-promoting complex/cyclosome-cdh1 mediates the ubiquitination and degradation of TRB3](/preview/png/1932980.png)
We have recently demonstrated that TRB3, a novel endoplasmic reticulum (ER) stress-inducible protein, is induced by CHOP and ATF4 to regulate their function and ER stress-induced cell death; however, the regulation of TRB3 function has not been well characterized. Here we demonstrate that TRB3 is an unstable protein regulated by the ubiquitin–proteasome system. The carboxyl-terminal domain of TRB3 is necessary for protein degradation, and in this region, we found the typical D-box motif, which is a critical sequence for the anaphase-promoting complex/cyclosome (APC/C) dependent proteolysis. TRB3 proteins were stabilized by deletion of its D-box motif and interacted with APC/C coactivator proteins, Cdc20 and Cdh1. The expression level of TRB3 protein is down-regulated by over-expression of Cdh1 but not by that of Cdc20. In addition, knockdown of Cdh1 enhanced the endogenous TRB3 expression level and suppressed its ubiquitination level. These results suggest that APC/CCdh1 is involved in ubiquitination and down-regulating the stability of TRB3 protein.
Journal: Biochemical and Biophysical Research Communications - Volume 392, Issue 3, 12 February 2010, Pages 289–294