Induction of Ptp2 and Cmp2 protein phosphatases is crucial for the adaptive response to ER stress in Saccharomyces cerevisiae.

Induction of Ptp2 and Cmp2 protein phosphatases is crucial for the adaptive response to ER stress in Saccharomyces cerevisiae.
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DOI:
10.1038/s41598-018-31413-6
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发表时间:
2018-08-30
期刊:
影响因子:
4.6
通讯作者:
Irie K
Irie K
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Mizuno T;Nakamura M;Irie K

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蛋白磷酸酶的表达调控与细胞信号传导的串扰和反馈密切相关。在芽殖酵母内质网应激反应中,多种信号通路被激活并在适应性反应中发挥关键作用。然而,目前还不清楚如何在ER应激反应过程中调节蛋白磷酸酶的表达水平。在这里,我们表明,ER应力增加表达的Ptp2酪氨酸磷酸酶和Cmp2钙调磷酸酶。Ptp2的上调是由于Mpk1 MAP激酶和Rlm1转录因子介导的转录激活。这种诱导对于Ptp2有效下调Hog1 MAP激酶的活性是重要的。芽殖酵母基因组具有两个基因,CMP 2和CNA 1,编码钙调磷酸酶的催化亚基。CMP 2不仅在内质网应激反应中比CNA 1更重要,而且在盐胁迫反应中也比CNA 1更重要。CMP 2启动子活性的提高有助于其在内质网应激反应中的相对功能意义,但对盐胁迫反应的重要性较小。因此,我们的研究结果表明,Ptp2和Cmp2蛋白磷酸酶在启动子水平的表达控制是至关重要的ER应激的适应性反应。
Expression control of the protein phosphatase is critically involved in crosstalk and feedback of the cellular signaling. In the budding yeast ER stress response, multiple signaling pathways are activated and play key roles in adaptive reactions. However, it remains unclear how the expression level of the protein phosphatase is modulated during ER stress response. Here, we show that ER stress increases expression of Ptp2 tyrosine phosphatase and Cmp2 calcineurin phosphatase. Upregulation of Ptp2 is due to transcriptional activation mediated by Mpk1 MAP kinase and Rlm1 transcription factor. This induction is important for Ptp2 to effectively downregulate the activity of Hog1 MAP kinase. The budding yeast genome possesses two genes, CMP2 and CNA1, encoding the catalytic subunit of calcineurin phosphatase. CMP2 is more important than CNA1 not only in ER stress response, but also in salt stress response. Higher promoter activity of CMP2 contributes to its relative functional significance in ER stress response, but is less important for salt stress response. Thus, our results suggest that expression control of Ptp2 and Cmp2 protein phosphatases at the promoter level is crucial for adaptive responses to ER stress.
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