Deconvoluting signals downstream of growth and immune receptor kinases by phosphocodes of the BSU1 family phosphatases.

Deconvoluting signals downstream of growth and immune receptor kinases by phosphocodes of the BSU1 family phosphatases.
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DOI:
10.1038/s41477-022-01167-1
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发表时间:
2022-06
期刊:
影响因子:
18
通讯作者:
Wang, Zhi-Yong
Wang, Zhi-Yong
中科院分区:
生物学1区
文献类型:
--
作者:
Park, Chan Ho;Bi, Yang;Youn, Ji-Hyun;Kim, So-Hee;Kim, Jung-Gun;Xu, Nicole Y.;Shrestha, Ruben;Burlingame, Alma L.;Xu, Shou-Ling;Mudgett, Mary Beth;Kim, Seong-Ki;Kim, Tae-Wuk;Wang, Zhi-Yong

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数百种富含亮氨酸的重复受体激酶(LRR-RKs)已经进化到控制植物生长、发育和免疫的各种过程;LRR-RKs与不同细胞反应之间的联系机制尚不清楚。本研究发现,油菜素内酯激素受体BRI1 (brassinosteroids INSENSITIVE 1)和鞭毛蛋白受体FLS2 (flagellin SENSING 2)这两个LRR-RKs分别通过磷酸化BRI1- suppressor1 (BSU1)磷酸酶来调控下游糖原合成酶激酶3 (GSK3)和丝裂原活化蛋白(MAP)激酶。BSU1先前被鉴定为BRI1通路中使gsk3失活的成分。我们惊奇地发现,BSU1家族磷酸酶的缺失激活了效应触发免疫(ETI),损害了鞭毛蛋白触发的MAP激酶激活和免疫。鞭毛蛋白激活的BOTRYTIS-INDUCED KINASE 1 (BIK1)磷酸化BSU1的丝氨酸-251位点。丝氨酸-251的突变会降低BSU1介导鞭毛蛋白诱导的MAP激酶激活和免疫的能力,但不会降低其抑制ETI和与GSK3相互作用的能力,GSK3通过BSU1在丝氨酸-764位点磷酸化油菜素内酯信号传导而增强。这些结果表明,BSU1在免疫中发挥重要作用,并通过不同的磷酸化位点转导油菜素类固醇- bri1和鞭毛蛋白- fls2信号。我们的研究表明,共享下游组分的磷酸化编码为多种植物受体激酶提供了信号特异性。
Hundreds of leucine-rich repeat receptor kinases (LRR-RKs) have evolved to control diverse processes of growth, development, and immunity in plants; the mechanisms that link LRR-RKs to distinct cellular responses are not understood. Here we show that two LRR-RKs, the brassinosteroid hormone receptor BRI1 (BRASSINOSTEROID INSENSITIVE 1) and the flagellin receptor FLS2 (FLAGELLIN SENSING 2), regulate downstream glycogen synthase kinase 3 (GSK3) and mitogen-activated protein (MAP) kinases, respectively, through phosphocoding of the BRI1-SUPPRESSOR1 (BSU1) phosphatase. BSU1 was previously identified as a component that inactivates GSK3s in the BRI1 pathway. We found surprisingly that loss of the BSU1 family phosphatases activates effector-triggered immunity (ETI) and impairs flagellin-triggered MAP kinase activation and immunity. The flagellin-activated BOTRYTIS-INDUCED KINASE 1 (BIK1) phosphorylates BSU1 at serine-251. Mutation of serine-251 reduces BSU1’s ability to mediate flagellin-induced MAP kinase activation and immunity, but not its abilities to suppress ETI and interact with GSK3, which is enhanced through the phosphorylation of BSU1 at serine-764 upon brassinosteroid signaling. These results demonstrate that BSU1 plays an essential role in immunity and transduces brassinosteroid-BRI1 and flagellin-FLS2 signals using different phosphorylation sites. Our study illustrates that phosphocoding in shared downstream components provides signaling specificities for diverse plant receptor kinases.
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