双次引发：细胞周期蛋白E在被泛素化之前先被磷酸化和异构化。

Twice primed: cyclin E is phosphorylated and isomerized before being ubiquitinated.

作者信息

Shumway Stuart D, Xiong Yue

机构信息

Lineberger Comprehensive Cancer Center, Department of Biochemistry and Biophysics, Program in Molecular Biology and Biotechnology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA.

出版信息

Mol Cell. 2006 Jul 21;23(2):149-50. doi: 10.1016/j.molcel.2006.07.002.

DOI:10.1016/j.molcel.2006.07.002

PMID:16857579

Abstract

Targeting proteins for irreversible degradation must be under tight control and is often regulated at the level of substrate-receptor binding. But does a protein really need to be marked twice with two different modifications, first phosphorylation and then isomerization, to bind its receptor, as van Drogen et al. (2006) show for cyclin E?

摘要

将蛋白质靶向不可逆降解必须受到严格控制，并且通常在底物 - 受体结合水平上进行调节。但是，正如范·德罗根等人（2006年）对细胞周期蛋白E所展示的那样，一种蛋白质真的需要先用磷酸化修饰，然后再用异构化修饰进行两次标记才能结合其受体吗？