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The UPR Branch IRE1- in Plants Plays an Essential Role in Viral Infection and Is Complementary to the Only UPR Pathway in Yeast
The unfolded protein response (UPR) is crucial to life as it regulates gene expression in response to stress in the endoplasmic reticulum (ER). There are two functionally overlapping UPR branches in plants, e.g., IRE1-bZIP60 and S1P/S2P-bZIP17/bZIP28, but only one, IRE1p-HAC1, in yeast. Despite recent significant progress in understanding UPR, a functional connectivity of IRE1 and its splicing target has not been established in multicellular eukaryotes. It is unknown if a single UPR branch in plants has any unique biological functions. Given that all eukaryotes are equipped with the IRE1-mediated pathway, are IRE1 downstream signaling effectors conserved among kingdoms and at what degree? Here, we show that IRE1 and its substrate bZIP60 function as a matched enzyme-substrate pair to mediate virus-host interactions in plants. We further provide evidence that a single UPR branch, IRE1-bZIP60, rather than S1P/S2P-bZIP17/bZIP28, determines viral pathogenesis, indicating that the two UPR arms may have distinct functions in plants. Finally, we demonstrate that the spliced form bZIP60 and HAC1p, rather than IRE1, are functionally replaceable to cope with abiotic stress in yeast, suggesting that the downstream signaling of the IRE1-mediated splicing is evolutionary conserved in plants and yeast. These data shed new lights into UPR in multicellular eukaryotes.
Vyšlo v časopise: The UPR Branch IRE1- in Plants Plays an Essential Role in Viral Infection and Is Complementary to the Only UPR Pathway in Yeast. PLoS Genet 11(4): e32767. doi:10.1371/journal.pgen.1005164
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.pgen.1005164Souhrn
The unfolded protein response (UPR) is crucial to life as it regulates gene expression in response to stress in the endoplasmic reticulum (ER). There are two functionally overlapping UPR branches in plants, e.g., IRE1-bZIP60 and S1P/S2P-bZIP17/bZIP28, but only one, IRE1p-HAC1, in yeast. Despite recent significant progress in understanding UPR, a functional connectivity of IRE1 and its splicing target has not been established in multicellular eukaryotes. It is unknown if a single UPR branch in plants has any unique biological functions. Given that all eukaryotes are equipped with the IRE1-mediated pathway, are IRE1 downstream signaling effectors conserved among kingdoms and at what degree? Here, we show that IRE1 and its substrate bZIP60 function as a matched enzyme-substrate pair to mediate virus-host interactions in plants. We further provide evidence that a single UPR branch, IRE1-bZIP60, rather than S1P/S2P-bZIP17/bZIP28, determines viral pathogenesis, indicating that the two UPR arms may have distinct functions in plants. Finally, we demonstrate that the spliced form bZIP60 and HAC1p, rather than IRE1, are functionally replaceable to cope with abiotic stress in yeast, suggesting that the downstream signaling of the IRE1-mediated splicing is evolutionary conserved in plants and yeast. These data shed new lights into UPR in multicellular eukaryotes.
Zdroje
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