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Phosphorylation by Casein Kinase 2 Regulates Nap1 Localization and Function

机译：酪蛋白激酶2的磷酸化调节Nap1本地化和功能。

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In Saccharomyces cerevisiae, the evolutionarily conserved nucleocytoplasmic shuttling protein Nap1 is a cofactor for the import of histones H2A and H2B, a chromatin assembly factor and a mitotic factor involved in regulation of bud formation. To understand the mechanism by which Nap1 function is regulated, Nap1-interacting factors were isolated and identified by mass spectrometry. We identified several kinases among these proteins, including casein kinase 2 (CK2), and a new bud neck-associated protein, Nba1. Consistent with our identification of the Nap1-interacting kinases, we showed that Nap1 is phosphorylated in vivo at 11 sites and that Nap1 is phosphorylated by CK2 at three substrate serines. Phosphorylation of these serines was not necessary for normal bud formation, but mutation of these serines to either alanine or aspartic acid resulted in cell cycle changes, including a prolonged S phase, suggesting that reversible phosphorylation by CK2 is important for cell cycle regulation. Nap1 can shuttle between the nucleus and cytoplasm, and we also showed that CK2 phosphorylation promotes the import of Nap1 into the nucleus. In conclusion, our data show that Nap1 phosphorylation by CK2 appears to regulate Nap1 localization and is required for normal progression through S phase.
机译：在酿酒酵母中，进化保守的核质穿梭蛋白Nap1是组蛋白H2A和H2B，染色质装配因子和有丝分裂因子参与芽形成调控的输入的辅因子。为了了解调节Nap1功能的机制，通过质谱法分离并鉴定了Nap1相互作用因子。我们在这些蛋白质中鉴定了几种激酶，包括酪蛋白激酶2（CK2）和新的芽颈相关蛋白Nba1。与我们对Nap1相互作用激酶的鉴定一致，我们表明Nap1在11个位点体内被磷酸化，而Nap1在三个底物丝氨酸上被CK2磷酸化。这些丝氨酸的磷酸化对于正常芽的形成不是必需的，但是这些丝氨酸突变为丙氨酸或天冬氨酸会导致细胞周期发生变化，包括延长的S期，这表明CK2可逆的磷酸化对于细胞周期的调控很重要。 Nap1可以在细胞核和细胞质之间穿梭，并且我们还显示CK2磷酸化促进Nap1进入细胞核。总之，我们的数据表明CK2的Nap1磷酸化似乎调节Nap1的定位，并且是S期正常进展所必需的。

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