Department of Biochemistry, College of Medicine, The Catholic University of Korea, Seoul, South Korea.
Curr Protein Pept Sci. 2012 Jun;13(4):331-6. doi: 10.2174/138920312801619411.
Post-transcriptional processes critically affect eukaryotic gene expression. Cells respond to environmental and intrinsic stresses by arresting global translation and inducing the accumulation of mRNAs into cytoplasmic RNA granules such as stress granules (SGs) and processing bodies (PBs), which are thought to participate in the regulation of translation and degradation of mRNAs. Stresses trigger the formation of SGs and increase PB size and abundance, and the two granules can share specific mRNAs and proteins. The protein content and dynamics of RNA granules have been extensively studied, but the mechanisms of interaction of RNA-binding proteins (RBPs) with binding partners and the signaling pathways that regulate these interactions are poorly understood. Post-translational modification of proteins in RNA granules via phosphorylation, glycosylation and methylation, influences their associations, enzymatic activities and intracellular locations. There is evidence that the post-translational modification of RBPs has a major influence on their binding to mRNA as well as on the assembly of RNA granules. In this review, recent findings concerning the post-translational modification of RBPs and their possible roles in the assembly of RNA granules are discussed.
转录后过程对真核生物基因表达具有至关重要的影响。细胞通过阻止全球翻译并诱导 mRNA 积累到细胞质 RNA 颗粒（如应激颗粒 (SGs) 和处理体 (PBs)）中来响应环境和内在压力，这些颗粒被认为参与了翻译的调节和 mRNA 的降解。应激会触发 SG 的形成并增加 PB 的大小和丰度，并且这两个颗粒可以共享特定的 mRNA 和蛋白质。RNA 颗粒的蛋白质含量和动力学已经得到了广泛的研究，但 RNA 结合蛋白 (RBP) 与结合伙伴相互作用的机制以及调节这些相互作用的信号通路仍知之甚少。通过磷酸化、糖基化和甲基化对 RNA 颗粒中的蛋白质进行翻译后修饰，会影响它们的相互作用、酶活性和细胞内位置。有证据表明，RBP 的翻译后修饰对它们与 mRNA 的结合以及 RNA 颗粒的组装有重大影响。在这篇综述中，讨论了关于 RBP 的翻译后修饰及其在 RNA 颗粒组装中的可能作用的最新发现。
