Molecular mechanism for the recognition of sequence-divergent CIF peptides by the plant receptor kinases GSO1/SGN3 and GSO2

Mis en avant

The plant leucine-rich repeat receptor kinases GSO1/SGN3 and its peptide ligands CIF1 and CIF2 are essential for the formation of the Casparian strip. The Hothorn group from the Department of Botany and Plant Biology, in collaboration with the Geldner group from UNIL, has now uncovered in molecular detail how the SCHENGEN 3 receptor complex tightly binds CIF1 and CIF2.

Crystal structure of the GSO1/SGN3–CIF complex reveals a binding pocket for sulfotyrosine and extended back-bone interactions with CIF2. Structure-guided sequence analysis allowed to uncover previously uncharacterized CIF peptides conserved among higher plants. Quantitative binding assays with known and novel CIFs suggest that the homologous LRR-RKs GSO1/SGN3 and GSO2 have evolved unique peptide binding properties to control different developmental processes. A quantitative biochemical interaction screen, a CIF peptide antagonist and genetic analyses together implicate SERK proteins as essential coreceptor kinases required for GSO1/SGN3 and GSO2 receptor activation.

This work provides a mechanistic framework for the recognition of sequence-divergent peptide hormones in plants and was published in PNAS on January 21, 2020.



由瑞士日内瓦大学科学学院教授 Thanos Halazonetis 领导的一项国际研究,揭示了癌细胞是如何修复受损的复制叉来完成细胞分裂的。这种称之为“断裂诱导复制” (BIR) 的信号通路在癌 细胞中常见,但却少见于健康细胞中。发表在 Science 杂志上的这项研究,由此揭示出了两种细胞类型之间的一个显著差异,作者们将尝试利用它来达到治疗 目的。

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