Human protein arginine methyltransferases in vivo - distinct properties of eight canonical members of the PRMT family
Human protein arginine methyltransferases in vivo - distinct properties of eight canonical members of the PRMT family
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DOI：
10.1242/jcs.039933
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发表时间：
2009-03-01
影响因子：
4
通讯作者：
Fackelmayer, Frank O.
中科院分区：
文献类型：
--
作者：
Herrmann, Frank;Pably, Peter;Fackelmayer, Frank O.
精氨酸甲基化是一种广泛存在的蛋白质翻译后修饰，由一个小家族的蛋白质精氨酸甲基转移酶（PRMT）催化。在功能上，修饰似乎调节蛋白质功能和影响基因调控、信号传导和蛋白质和核酸的亚细胞定位的相互作用。所有成员已在不同程度上，其特征在于单独和它们的含义在细胞过程中已推断出表征基板和相互作用。在这里，我们报告的第一次全面比较的所有8个典型的人类PRMT家族成员在活细胞中的亚细胞定位和动态。我们表明，个别家庭成员显着不同的性质，以及在其底物的特异性，这表明他们履行独特的，非冗余的功能在体内。此外，某些PRMT在不同的细胞类型中显示不同的亚细胞定位，暗示调节PRMT功能的细胞和组织特异性机制。
Methylation of arginine residues is a widespread post-translational modification of proteins catalyzed by a small family of protein arginine methyltransferases (PRMTs). Functionally, the modification appears to regulate protein functions and interactions that affect gene regulation, signalling and subcellular localization of proteins and nucleic acids. All members have been, to different degrees, characterized individually and their implication in cellular processes has been inferred from characterizing substrates and interactions. Here, we report the first comprehensive comparison of all eight canonical members of the human PRMT family with respect to subcellular localization and dynamics in living cells. We show that the individual family members differ significantly in their properties, as well as in their substrate specificities, suggesting that they fulfil distinctive, non-redundant functions in vivo. In addition, certain PRMTs display different subcellular localization in different cell types, implicating cell- and tissue-specific mechanisms for regulating PRMT functions.