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Title   Ubiquitin - Proteasome 경로에 의한 Retinoblastoma Family Protein P107 의 단백 분해에 관한 연구 ( Proteolytic Regulation of Retinoblastoma Family Protein p107 by Ubiquitin - proteasome Pathway )
Publicationinfo   2000 Jan; 032(02): 417-422.
Key_word   p107 protein, Proteolysis, Ubiquitin-proteasome pathway
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Abstract   Purpose: Proteolysis is an important way to regulate cell cycle regulatory proteins. Ubiquitin- proteasome pathway regards as highly selective proteolytic machinary mostly in physiological state. We investigated the role of ubiquitin-proteasome pathway in p107 protein degradation. Materials and Methods: p107 protein level was determined by western blot analysis in Ewings sarcoma cell line incubated with HMG-CoA inhibitor lovastatin. Recovery of p107 protein was determined with inhibitors of proteasome, serine protease or caspase. Ubiquitination of p107 protein was assessed by ubiquitin western analysis. Results: pl07 protein level was decreased with lovastin and its proteolytic effect was counteracted with proteasome inhibitors. Ubiquitin western analysis showed p107 protein fragments were tagged with ubiquitin and it was more evident with specific proteasome inhibitor lactacystin. Conclusion: Lovastatin drives p107 protein to be degraded. In a certain circumstance proteolysis of p107 protein was executed by ubiquitin-proteasome pathway.
저 자   장정순(Joung Soon Jang),박병규(Byung Kyu Park),황상구(Sang Gu Hwang)