کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1939917 | 1050770 | 2006 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: MYO18B interacts with the proteasomal subunit Sug1 and is degraded by the ubiquitin–proteasome pathway MYO18B interacts with the proteasomal subunit Sug1 and is degraded by the ubiquitin–proteasome pathway](/preview/png/1939917.png)
MYO18B is a class XVIIIB unconventional myosin encoded by a candidate tumor suppressor gene. To gain insights into the cellular function of this protein, we searched for MYO18B-interacting proteins by a yeast two-hybrid screen. Sug1, a 19S regulator subunit of the 26S proteasome, was identified as a binding partner of the C-terminal tail region of MYO18B. The association of MYO18B with Sug1 was further confirmed by GST pull-down, co-immunoprecipitation, and immunocytochemistry. Furthermore, proteasome dysfunction by a proteasome inhibitor or siRNA-mediated knock-down of Sug1 caused the up-regulation of MYO18B protein and MYO18B was polyubiquitinated in vivo. Collectively, these results suggested that MYO18B is a substrate for proteasomal degradation.
Journal: Biochemical and Biophysical Research Communications - Volume 342, Issue 3, 14 April 2006, Pages 829–834