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首页> 美国卫生研究院文献>PLoS Genetics >The UPR Branch IRE1-bZIP60 in Plants Plays an Essential Role in Viral Infection and Is Complementary to the Only UPR Pathway in Yeast
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The UPR Branch IRE1-bZIP60 in Plants Plays an Essential Role in Viral Infection and Is Complementary to the Only UPR Pathway in Yeast

机译：植物中的UPR分支IRE1-bZIP60在病毒感染中起重要作用并补充了酵母中唯一的UPR途径

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The unfolded protein response (UPR) signaling network encompasses two pathways in plants, one mediated by inositol-requiring protein-1 (IRE1)-bZIP60 mRNA and the other by site-1/site-2 proteases (S1P/S2P)-bZIP17/bZIP28. As the major sensor of UPR in eukaryotes, IRE1, in response to endoplasmic reticulum (ER) stress, catalyzes the unconventional splicing of HAC1 in yeast, bZIP60 in plants and XBP1 in metazoans. Recent studies suggest that IRE1p and HAC1 mRNA, the only UPR pathway found in yeast, evolves as a cognate system responsible for the robust UPR induction. However, the functional connectivity of IRE1 and its splicing target in multicellular eukaryotes as well as the degree of conservation of IRE1 downstream signaling effectors across eukaryotes remains to be established. Here, we report that IRE1 and its substrate bZIP60 function as a strictly cognate enzyme-substrate pair to control viral pathogenesis in plants. Moreover, we show that the S1P/S2P-bZIP17/bZIP28 pathway, the other known branch of UPR in plants, does not play a detectable role in virus infection, demonstrating the distinct function of the IRE1-bZIP60 pathway in plants. Furthermore, we provide evidence that bZIP60 and HAC1, products of the enzyme-substrate duet, rather than IRE1, are functionally replaceable to cope with ER stress in yeast. Taken together, we conclude that the downstream signaling of the IRE1-mediated splicing is evolutionarily conserved in yeast and plants, and that the IRE1-bZIP60 UPR pathway not only confers overlapping functions with the other UPR branch in fundamental biology but also may exert a unique role in certain biological processes such as virus-plant interactions.
机译：未折叠的蛋白质反应（UPR）信号网络涵盖植物中的两条途径，一条途径由需要肌醇的Protein-1（IRE1）-bZIP60 mRNA介导，另一条途径由site-1 / site-2蛋白酶（S1P / S2P）-bZIP17 / bZIP28。 IRE1作为真核生物中UPR的主要传感器，响应内质网（ER）胁迫，催化酵母中HAC1，植物bZIP60和后生动物XBP1的非常规剪接。最近的研究表明，IRE1p和HAC1 mRNA是在酵母中发现的唯一UPR途径，其进化为同源系统，负责强大的UPR诱导。但是，IRE1及其剪接靶标在多细胞真核生物中的功能连接性以及跨真核生物的IRE1下游信号传导效应子的保守程度仍有待确定。在这里，我们报告IRE1及其底物bZIP60充当严格同源的酶-底物对，以控制植物的病毒发病机理。此外，我们显示了S1P / S2P-bZIP17 / bZIP28途径，植物中UPR的另一个已知分支，在病毒感染中没有可检测的作用，证明了IRE1-bZIP60途径在植物中的独特功能。此外，我们提供的证据表明，酶底物二重产物而不是IRE1的bZIP60和HAC1在功能上可替代，以应对酵母中的内质网应激。两者合计，我们得出结论，IRE1介导的剪接的下游信号在酵母和植物中是进化保守的，并且IRE1-bZIP60 UPR途径不仅赋予基础生物学中其他UPR分支重叠的功能，而且可能发挥独特的作用在某些生物过程中的作用，例如病毒与植物的相互作用。

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