Dai Mu-Shui, Jin Yetao, Gallegos Jayme R, Lu Hua
Department of Biochemistry and Molecular Biology, School of Medicine, Oregon Health and Science University, Portland, OR 97239, USA.
Neoplasia. 2006 Aug;8(8):630-44. doi: 10.1593/neo.06334.
Protein ubiquitylation has been demonstrated to play a vital role not only in mediating protein turnover but also in modulating protein activity. The stability and activity of the tumor suppressor p53 and of the oncoprotein c-Myc are no exception. Both are regulated through independent ubiquitylation by several E3 ubiquitin ligases. Interestingly, p53 and c-Myc are functionally connected by some of these E3 enzymes and their regulator ARF, although these proteins play opposite roles in controlling cell growth and proliferation. The balance of this complex ubiquitylation network and its disruption during oncogenesis will be the topics of this review.
蛋白质泛素化不仅在介导蛋白质周转中起关键作用，还在调节蛋白质活性方面发挥重要作用。肿瘤抑制因子p53和癌蛋白c-Myc的稳定性和活性也不例外。二者均通过几种E3泛素连接酶进行独立的泛素化调节。有趣的是，尽管这些蛋白质在控制细胞生长和增殖中发挥相反作用，但p53和c-Myc在功能上通过其中一些E3酶及其调节因子ARF相互联系。这个复杂的泛素化网络的平衡及其在肿瘤发生过程中的破坏将是本综述的主题。
