Inhibition of Transcription Induces Phosphorylation of YB-1 at Ser102 and Its Accumulation in the Nucleus
Inhibition of Transcription Induces Phosphorylation of YB-1 at Ser102 and Its Accumulation in the Nucleus
复制标题
DOI：
10.3390/cells9010104
复制
发表时间：
2020-01-01
期刊：
影响因子：
6
通讯作者：
Ovchinnikov, Lev P.
中科院分区：
文献类型：
--
作者：
Kretov, Dmitry A.;Mordovkina, Daria A.;Ovchinnikov, Lev P.
Y-box结合蛋白1 （YB-1）是调控细胞质和细胞核中基因表达的RNA/ dna结合蛋白。虽然主要是细胞质，但在胁迫条件下，YB-1在细胞核中积累。它的核定位与癌细胞的侵袭性和多药耐药有关，这使得了解YB-1亚细胞分布的调控机制至关重要。在这里，我们报道了RNA聚合酶II （RNAPII）活性的抑制导致YB-1的核积累，并伴随其Ser102位点的磷酸化。激酶活性的抑制减少了YB-1磷酸化及其在细胞核中的积累。RNA在细胞核中的存在被证明是YB-1的核保留所必需的。因此，YB-1的亚细胞定位取决于其翻译后修饰（PTMs）和细胞内RNA分布。
The Y-box binding protein 1 (YB-1) is an RNA/DNA-binding protein regulating gene expression in the cytoplasm and the nucleus. Although mostly cytoplasmic, YB-1 accumulates in the nucleus under stress conditions. Its nuclear localization is associated with aggressiveness and multidrug resistance of cancer cells, which makes the understanding of the regulatory mechanisms of YB-1 subcellular distribution essential. Here, we report that inhibition of RNA polymerase II (RNAPII) activity results in the nuclear accumulation of YB-1 accompanied by its phosphorylation at Ser102. The inhibition of kinase activity reduces YB-1 phosphorylation and its accumulation in the nucleus. The presence of RNA in the nucleus is shown to be required for the nuclear retention of YB-1. Thus, the subcellular localization of YB-1 depends on its post-translational modifications (PTMs) and intracellular RNA distribution.