6a5b | pdb_00006a5b
Crystal structure of plant Receptor-like Kinase FER
Structural highlights
FunctionFERON_ARATH Receptor-like protein kinase that mediates the female control of male gamete delivery during fertilization, including growth cessation of compatible pollen tubes ensuring a reproductive isolation barriers, by regulating MLO7 subcellular polarization upon pollen tube perception in the female gametophyte synergids. Required for cell elongation during vegetative growth, mostly in a brassinosteroids- (BR-) independent manner. Acts as an upstream regulator for the Rac/Rop-signaling pathway that controls ROS-mediated root hair development. Seems to regulate a cross-talk between brassinosteroids and ethylene signaling pathways during hypocotyl elongation. Negative regulator of brassinosteroid response in light-grown hypocotyls, but required for brassinosteroid response in etiolated seedlings. Mediates sensitivity to powdery mildew (e.g. Golovinomyces orontii). Positive regulator of auxin-promoted growth that represses the abscisic acid (ABA) signaling via the activation of ABI2 phosphatase. Required for RALF1-mediated extracellular alkalinization in a signaling pathway preventing cell expansion.[1] [2] [3] [4] [5] [6] [7] Publication Abstract from PubMedReceptor kinases of the Catharanthus roseus RLK1-like (CrRLK1L) family have emerged as important regulators of plant reproduction, growth and responses to the environment(1). Endogenous RAPID ALKALINIZATION FACTOR (RALF) peptides(2) have previously been proposed as ligands for several members of the CrRLK1L family(1). However, the mechanistic basis of this perception is unknown. Here we report that RALF23 induces a complex between the CrRLK1L FERONIA (FER) and LORELEI (LRE)-LIKE GLYCOSYLPHOSPHATIDYLINOSITOL (GPI)-ANCHORED PROTEIN 1 (LLG1) to regulate immune signalling. Structural and biochemical data indicate that LLG1 (which is genetically important for RALF23 responses) and the related LLG2 directly bind RALF23 to nucleate the assembly of RALF23-LLG1-FER and RALF23-LLG2-FER heterocomplexes, respectively. A conserved N-terminal region of RALF23 is sufficient for the biochemical recognition of RALF23 by LLG1, LLG2 or LLG3, and binding assays suggest that other RALF peptides that share this conserved N-terminal region may be perceived by LLG proteins in a similar manner. Structural data also show that RALF23 recognition is governed by the conformationally flexible C-terminal sides of LLG1, LLG2 and LLG3. Our work reveals a mechanism of peptide perception in plants by GPI-anchored proteins that act together with a phylogenetically unrelated receptor kinase. This provides a molecular framework for understanding how diverse RALF peptides may regulate multiple processes, through perception by distinct heterocomplexes of CrRLK1L receptor kinases and GPI-anchored proteins of the LRE and LLG family. Mechanisms of RALF peptide perception by a heterotypic receptor complex.,Xiao Y, Stegmann M, Han Z, DeFalco TA, Parys K, Xu L, Belkhadir Y, Zipfel C, Chai J Nature. 2019 Aug;572(7768):270-274. doi: 10.1038/s41586-019-1409-7. Epub 2019 Jul , 10. PMID:31291642[8] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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