A receptor heteromer mediates the male perception of female attractants in plants

• Published in: Nature (London) Vol. 531; no. 7593; pp. 241 - 244
• Main Authors: Wang, Tong, Liang, Liang, Xue, Yong, Jia, Peng-Fei, Chen, Wei, Zhang, Meng-Xia, Wang, Ying-Chun, Li, Hong-Ju, Yang, Wei-Cai
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 10.03.2016; Nature Publishing Group
• Subjects: 631/449/2675; 631/449/2679/2113; Angiosperms; Arabidopsis - genetics; Arabidopsis - metabolism; Arabidopsis - physiology; Arabidopsis Proteins - chemistry; Arabidopsis Proteins - genetics; Arabidopsis Proteins - metabolism; Attractants; Botany; Capsella - genetics; Capsella - metabolism; Capsella - physiology; Cell Membrane - metabolism; Females; Flowering plants; Flowers & plants; Genetic aspects; Humanities and Social Sciences; Kinases; letter; multidisciplinary; Mutation; Ovule - metabolism; Peptides; Phenotype; Phosphorylation; Phosphotransferases - chemistry; Phosphotransferases - genetics; Phosphotransferases - metabolism; Plant reproduction; Pollen; Pollen Tube - genetics; Pollen Tube - growth & development; Pollen Tube - metabolism; Protein Kinases - genetics; Protein Kinases - metabolism; Protein Multimerization; Protein Structure, Quaternary; Protein Structure, Tertiary; Receptors, Cell Surface - chemistry; Receptors, Cell Surface - genetics; Receptors, Cell Surface - metabolism; Reproduction; Science; Signal Transduction; United States
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/nature16975

A male cell-surface receptor-like kinase that responds to the female chemoattractant LURE1 on the pollen tube of Arabidopsis thaliana is identified; LURE1 triggers dimerization of the receptor components and activation of the kinase activity, and the transformation of a component of the A. thaliana receptor to the Capsella rubella species partially breaks down the reproductive isolation barrier. Multiple pollen-tube receptors for LURE1 In flowering plants, the female gametophyte secretes chemoattractant peptides to guide pollen tube growth so that it delivers the immobile sperm to the ovule-enclosed female gametophyte. Two papers published in this issue of Nature report the identification of male pollen tube cell-surface receptors for one of these female attractants, LURE1, in the model plant Arabidopsis thaliana . Wei-Cai Yang and colleagues show that LURE1 is perceived by a receptor-like kinase complex, the heteromer MDIS1–MIK. Tetsuya Higashiyama and Hidenori Takeuchi report that pollen-specific receptor-like kinase 6 (PRK6) is required for sensing LURE1, and PRK6 acts together with other PRK family receptors. Both groups demonstrate that by engineering pollen tubes of the sister species Capsella rubella to express a component of the A. thaliana receptors — either MDIS1 or PRK6 — the reproductive isolation barrier between the two species is partially broken down. Sexual reproduction requires recognition between the male and female gametes. In flowering plants, the immobile sperms are delivered to the ovule-enclosed female gametophyte by guided pollen tube growth. Although the female gametophyte-secreted peptides have been identified to be the chemotactic attractant to the pollen tube 1 , 2 , 3 , the male receptor(s) is still unknown. Here we identify a cell-surface receptor heteromer, MDIS1–MIK, on the pollen tube that perceives female attractant LURE1 in Arabidopsis thaliana . MDIS1, MIK1 and MIK2 are plasma-membrane-localized receptor-like kinases with extracellular leucine-rich repeats and an intracellular kinase domain. LURE1 specifically binds the extracellular domains of MDIS1, MIK1 and MIK2, whereas mdis1 and mik1 mik2 mutant pollen tubes respond less sensitively to LURE1. Furthermore, LURE1 triggers dimerization of the receptors and activates the kinase activity of MIK1. Importantly, transformation of At MDIS1 to the sister species Capsella rubella can partially break down the reproductive isolation barrier. Our findings reveal a new mechanism of the male perception of the female attracting signals.