A phosphorylation-driven ubiquitination switch for cell-cycle control
A phosphorylation-driven ubiquitination switch for cell-cycle control
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DOI：
10.1016/s0962-8924(01)02238-3
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发表时间：
2002-03-01
影响因子：
19
通讯作者：
Harper, JW
中科院分区：
文献类型：
--
作者：
Harper, JW
细胞状态的变化可以由超敏感蛋白激酶级联、正反馈环路和其他机制构建的复杂的全有或全无开关决定。最近的研究表明，通过 SCF 泛素连接酶途径磷酸化驱动的蛋白质破坏也可以以类似开关的方式发生。在这种情况下，多个磷酸化事件用于设置底物靶向的阈值，从而为理解蛋白质磷酸化和泛素介导的蛋白水解之间的相互关系提供框架。
Cellular changes in state can be dictated by complex all-or-nothing switches built from ultrasensitive protein kinase cascades, positive-feed back loops and other mechanisms. Recent work has established that phosphorylation-driven protein destruction through the SCF ubiquitin-ligase pathway can also occur in a switch-like manner. In this context, multiple phosphorylation events are used to set a threshold for substrate targeting, thereby providing a framework for understanding the inter-relationship between protein phosphorylation and ubiquitin-mediated proteolysis.