Smyd2 controls cytoplasmic lysine methylation of Hsp90 and myofilament organization
Smyd2 controls cytoplasmic lysine methylation of Hsp90 and myofilament organization
复制标题
DOI：
10.1101/gad.177758.111
复制
发表时间：
2012-01-15
影响因子：
10.5
通讯作者：
Linke, Wolfgang A.
中科院分区：
文献类型：
--
作者：
Donlin, Laura T.;Andresen, Christian;Linke, Wolfgang A.
蛋白质赖氨酸甲基化是真核细胞核中最广泛的翻译后修饰之一。组蛋白和非组蛋白上的甲基化赖氨酸促进控制基因表达和DNA复制和修复的蛋白质复合物的形成。然而，在细胞质中，赖氨酸甲基化在蛋白质复合物形成中的作用还没有很好地确定。在这里，我们报告的细胞质蛋白伴侣热休克蛋白90是甲基化的赖氨酸甲基转移酶Smyd2在各种类型的细胞。在肌肉中，Hsp90甲基化有助于形成含有Smyd2、Hsp90和肌节蛋白titin的蛋白质复合物。Smyd2缺陷导致Hsp90甲基化丧失、肌联蛋白稳定性受损和肌肉功能改变。总的来说，我们的数据揭示了一个细胞质蛋白质网络，采用赖氨酸甲基化的骨骼肌的维护和功能。
Protein lysine methylation is one of the most widespread post-translational modifications in the nuclei of eukaryotic cells. Methylated lysines on histones and nonhistone proteins promote the formation of protein complexes that control gene expression and DNA replication and repair. In the cytoplasm, however, the role of lysine methylation in protein complex formation is not well established. Here we report that the cytoplasmic protein chaperone Hsp90 is methylated by the lysine methyltransferase Smyd2 in various cell types. In muscle, Hsp90 methylation contributes to the formation of a protein complex containing Smyd2, Hsp90, and the sarcomeric protein titin. Deficiency in Smyd2 results in the loss of Hsp90 methylation, impaired titin stability, and altered muscle function. Collectively, our data reveal a cytoplasmic protein network that employs lysine methylation for the maintenance and function of skeletal muscle.