Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, Bethesda, Maryland 20892, USA.
Cell Biosci. 2011 Dec 28;1(1):43. doi: 10.1186/2045-3701-1-43.
Transforming growth factor-β (TGF-β) signaling is tightly regulated at the level of post-translational modification to transmit quantitative difference in ligand concentration into proportional transcriptional output. Ubiquitination is one such modification with several E3 ubiquitin ligases implicated in TGF-β signaling in marking crucial pathway components for proteasomal degradation. However, ubiquitination, particularly in the mono- or oligo-ubiquitin modifying form, is also known to regulate incorporation of substrate proteins into signaling complexes that involved in DNA repair, kinase activation, and endocytosis. This review focuses on recent advances in understanding the role of such non-degradative ubiquitination in TGF-β signaling.
转化生长因子-β（TGF-β）信号在翻译后修饰水平上受到严格调控，将配体浓度的定量差异传递到比例转录输出中。泛素化是一种这样的修饰，有几种 E3 泛素连接酶参与 TGF-β信号转导，标记关键途径成分进行蛋白酶体降解。然而，泛素化，特别是单泛素或寡泛素修饰形式，也被认为调节底物蛋白掺入涉及 DNA 修复、激酶激活和内吞作用的信号复合物中。这篇综述重点介绍了近年来对 TGF-β信号中非降解泛素化作用的理解的进展。
