Shedding light on autophagy coordinating with cell wall integrity signaling to govern pathogenicity of Magnaporthe oryzae

Shedding light on autophagy coordinating with cell wall integrity signaling to govern pathogenicity of Magnaporthe oryzae
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揭示自噬与细胞壁完整性信号协调控制稻瘟病菌的致病性

DOI:
10.1080/15548627.2019.1644075
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发表时间:
2019-07-25
期刊:
影响因子:
13.3
通讯作者:
Zhang, Zhengguang
Zhang, Zhengguang
中科院分区:
生物学1区
文献类型:
--
作者:
Yin, Ziyi;Feng, Wanzhen;Zhang, Zhengguang

文献摘要

相似文献

细胞在生长发育过程中面临着各种应激,细胞自噬是细胞在这些应激条件下分解自身成分回收大分子并提供能量的一种降解过程。对于利用细胞壁作为抵抗外部胁迫的第一道屏障的病原真菌来说,细胞壁完整性(CWI)途径也在应对这些胁迫中发挥了重要作用。然而,自噬与CWI之间的具体联系在包括出芽酵母(Saccharomyces cerevisiae)和稻瘟病菌(Magnaporthe oryzae)在内的模式真菌中仍不清楚。在这里,我们提供了证据,证明内质网(ER)应激在m.o ryzae感染期间被高度诱导,并且CWI MAP激酶激酶MoMkk1 (S. cerevisiae Mkk1/2同源物)受MoAtg1的磷酸化调节,MoAtg1是核心自噬机制中唯一被鉴定的激酶。我们还发现MoMkk1丝氨酸115是moatg1依赖的磷酸化位点,这种磷酸化可以激活CWI,类似于保守的MAP激酶激酶MoMck1激酶(酿酒酵母Bck1同源物)。我们首次报道了MoMkk1受MoAtg1磷酸化调控,揭示了内质网胁迫下自噬与CWI信号协调的新机制,并且这种依赖MoAtg1的MoMkk1磷酸化对m.o ryzae的致病性至关重要。缩写:A/Ala:丙氨酸;Atg: autophagy-related;Bck1: C激酶1旁路;co-IP: co-immunoprecipitation;CWI:细胞壁完整性;德勤:二硫苏糖醇;ER:内质网;GFP:绿色荧光蛋白;莫:稻谷;MAPK:丝裂原活化蛋白激酶;Mkk1:丝裂原活化蛋白激酶1;MS:质谱法;PAS:噬菌体组装位点;RFP:红色荧光蛋白;RT:室温;S / Ser:丝氨酸;Slt2:裂解型2的抑制因子;T /刺:苏氨酸;UPR:未折叠蛋白反应;Y2H:酵母双杂交筛。
ABSTRACT Cells are faced with various stresses during their growth and development, and autophagy is a degradative process in which cells can break down their own components to recycle macromolecules and provide energy under these stresses. For pathogenic fungi that utilize cell wall as the first barrier against external stress, the cell wall integrity (CWI) pathway also provides an essential role in responding to these stresses. However, the specific connection between autophagy and CWI remains elusive in either the model fungi including budding yeast Saccharomyces cerevisiae or the rice blast fungus Magnaporthe oryzae. Here, we provided evidence that the endoplasmic reticulum (ER) stress is highly induced during M. oryzae infection and that CWI MAP kinase kinase MoMkk1 (S. cerevisiae Mkk1/2 homolog) was subject to phosphorylation regulation by MoAtg1, the only identified kinase in the core autophagy machinery. We also identified MoMkk1 serine 115 as the MoAtg1-dependent phosphorylation site and this phosphorylation could activate CWI, similar to that by the conserved MAP kinase kinase kinase MoMck1 (S. cerevisiae Bck1 homolog). Together with the first report of MoMkk1 subjects to phosphorylation regulation by MoAtg1, we revealed a new mechanism by which autophagy coordinates with CWI signaling under ER stress, and this MoAtg1-dependent MoMkk1 phosphorylation is essential for the pathogenicity of M. oryzae. Abbreviations: A/Ala: alanine; Atg: autophagy-related; Bck1: bypass of C kinase 1; co-IP: co-immunoprecipitation; CWI: cell wall integrity;DTT: dithiothreitol; ER: endoplasmic reticulum; GFP: green fluorescent protein; Mo: Magnaporthe oryzae; MAPK: mitogen-activated protein kinase; Mkk1: mitogen-activated protein kinase-kinase 1; MS: mass spectrometry; PAS: phagophore assembly site; RFP: red fluorescent protein; RT: room temperature; S/Ser: serine; Slt2: suppressor of the lytic phenotype 2; T/Thr: threonine; UPR: unfolded protein response; Y2H: yeast two-hybrid screen.