Pastor Florentin, Shkreta Lulzim, Chabot Benoit, Durantel David, Salvetti Anna
International Center for Infectiology Research (CIRI), INSERM U1111, CNRS UMR5308, Université de Lyon (UCBL1), Lyon, France.
Department of Microbiology and Infectious Diseases, Faculty of Medicine and Health Sciences, Université de Sherbrooke, Sherbrooke, QC, Canada.
Front Microbiol. 2021 Mar 29;12:658721. doi: 10.3389/fmicb.2021.658721. eCollection 2021.
Protein phosphorylation constitutes a major post-translational modification that critically regulates the half-life, intra-cellular distribution, and activity of proteins. Among the large number of kinases that compose the human kinome tree, those targeting RNA-binding proteins, in particular serine/arginine-rich (SR) proteins, play a major role in the regulation of gene expression by controlling constitutive and alternative splicing. In humans, these kinases belong to the CMGC [Cyclin-dependent kinases (CDKs), Mitogen-activated protein kinases (MAPKs), Glycogen synthase kinases (GSKs), and Cdc2-like kinases (CLKs)] group and several studies indicate that they also control viral replication direct or indirect mechanisms. The aim of this review is to describe known and emerging activities of CMGC kinases that share the common property to phosphorylate SR proteins, as well as their interplay with different families of viruses, in order to advance toward a comprehensive knowledge of their pro- or anti-viral phenotype and better assess possible translational opportunities.
蛋白质磷酸化是一种主要的翻译后修饰，对蛋白质的半衰期、细胞内分布和活性起着关键的调节作用。在构成人类激酶组树的大量激酶中，那些靶向RNA结合蛋白，特别是富含丝氨酸/精氨酸（SR）的蛋白的激酶，通过控制组成型和可变剪接在基因表达调控中发挥主要作用。在人类中，这些激酶属于CMGC[细胞周期蛋白依赖性激酶（CDK）、丝裂原活化蛋白激酶（MAPK）、糖原合酶激酶（GSK）和Cdc2样激酶（CLK）]组，多项研究表明它们还通过直接或间接机制控制病毒复制。本综述的目的是描述CMGC激酶的已知和新出现的活性，这些激酶具有磷酸化SR蛋白的共同特性，以及它们与不同病毒家族的相互作用，以便更全面地了解它们的抗病毒或促病毒表型，并更好地评估可能的转化机会。
