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甾醇感应受体激酶通过与营养缺陷型中的 elicitins 偶联来感知甾醇。

A receptor kinase senses sterol by coupling with elicitins in auxotrophic .

机构信息

Department of Plant Pathology, Nanjing Agricultural University, Nanjing 210095, China.

Bioinformatics Center, Academy for Advanced Interdisciplinary Studies, Nanjing Agricultural University, Nanjing 210095, China.

出版信息

Proc Natl Acad Sci U S A. 2024 Nov 5;121(45):e2408186121. doi: 10.1073/pnas.2408186121. Epub 2024 Oct 30.

Abstract

Sterols are vital nutrients and signals for eukaryotic organisms. Mammalian cells are known to sense and respond to sterol status changes to maintain them within strict limits, a process associated with various human diseases. However, this process is not understood in oomycete pathogens, most of which are sterol auxotrophic and must obtain sterols from host plants. Here, we report that SSRK1 (sterol-sensing receptor kinase 1) detects host sterols by coupling with elicitins, thereby controlling signaling and sterol absorption. Sterols are recruited by extracellular soluble elicitins, and these complexes then bind to SSRK1 to form trimolecular complexes. These complexes subsequently trigger downstream calcium influx, activation of mitogen-activated protein kinase, and transcriptome reprogramming through the receptor's kinase activity. Our data demonstrate a unique sterol sensing pathway where elicitins and a transmembrane receptor kinase SSRK1 act as coreceptors for extracellular sterols. These findings also portray a sterol-based war between oomycetes and plants, providing a unique perspective on how a pathogen detects host signals during infection.

摘要

甾醇是真核生物的重要营养物质和信号分子。已知哺乳动物细胞能够感知和响应甾醇状态的变化,以将其维持在严格的限制范围内,这一过程与各种人类疾病有关。然而,在卵菌病原体中,这一过程尚不清楚,大多数卵菌都是甾醇营养缺陷型的,必须从宿主植物中获取甾醇。在这里,我们报告 SSRK1(甾醇感应受体激酶 1)通过与激发素偶联来检测宿主甾醇,从而控制信号转导和甾醇吸收。甾醇被细胞外可溶性激发素募集,然后这些复合物与 SSRK1 结合形成三聚体复合物。这些复合物随后通过受体的激酶活性触发下游钙内流、丝裂原活化蛋白激酶的激活和转录组重编程。我们的数据表明了一种独特的甾醇感应途径,其中激发素和跨膜受体激酶 SSRK1 作为细胞外甾醇的核心受体发挥作用。这些发现还描绘了卵菌和植物之间基于甾醇的战争,为病原体在感染过程中如何检测宿主信号提供了独特的视角。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3daa/11551405/b8fb8af60882/pnas.2408186121fig01.jpg

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