a Department of Pharmacology , University of Colorado School of Medicine , Aurora , CO , USA.
b Center for Epigenetics Van Andel Research Institute , Grand Rapids , MI , USA.
Crit Rev Biochem Mol Biol. 2019 Feb;54(1):1-10. doi: 10.1080/10409238.2018.1564730. Epub 2019 Jan 28.
Although relatively small in size, the ZZ-type zinc finger (ZZ) domain is a versatile signaling module that is implicated in a diverse set of cell signaling events. Here, we highlight the most recent studies focused on the ZZ domain function as a histone reader and a sensor of protein degradation signals. We review and compare the molecular and structural mechanisms underlying targeting the amino-terminal sequences of histone H3 and arginylated substrates by the ZZ domain. We also discuss the ZZ domain sensitivity to histone PTMs and summarize biological outcomes associated with the recognition of histone and non-histone ligands by the ZZ domain-containing proteins and complexes.
虽然 ZZ 型锌指 (ZZ) 结构域体积相对较小，但它是一种多功能的信号模块，涉及多种细胞信号事件。在这里，我们重点介绍了最近关于 ZZ 结构域作为组蛋白阅读器和蛋白质降解信号传感器功能的研究。我们回顾并比较了 ZZ 结构域靶向组蛋白 H3 氨基末端序列和精氨酸化底物的分子和结构机制。我们还讨论了 ZZ 结构域对组蛋白 PTM 的敏感性，并总结了与 ZZ 结构域蛋白和复合物识别组蛋白和非组蛋白配体相关的生物学结果。
