Abstract
Plant hormones are a set of small organic compounds that play a key role in plant growth, development, and responses to environmental signals. In addition to these conventional hormones, recent studies have revealed physiologically crucial roles of peptide hormones. Plant hormone receptors comprise different types of proteins including F-box proteins, an adaptor protein of F-box protein, a protein phosphatase inhibitor, histidine kinases, and Ser/Thr receptor kinases. In certain cases, receptors of gibberellin, strigolactone and karrikin are folded into α/β hydrolase folds, and the strigolactone and karrikin receptors possess a conserved catalytic triad system and preserved hydrolase activity. Plant hormones are allosteric inducers that induce conformational changes in receptors upon hormone perception to switch on or facilitate the transfer of signals to downstream effector proteins. To accomplish the switch function, plant hormone receptors adopt several mechanisms such as the “molecular glue” mechanism of the auxin and jasmonate receptors, or the “close-the-lid” and the “gate-latch-lock” mechanisms of the gibberellin and abscisic acid receptors, respectively. The brassinosteroid receptor and certain peptide receptors also adopt the “molecular glue” mechanism for co-receptor binding.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Cardozo T, Pagano MM (2004) The SCF Ubiquitin ligase: insights into a molecular machine. Nat Rev Mol Cell Biol 5:739–751
Chow B, McCourt P (2006) Plant hormone receptors: perception is everything. Genes Dev 20:1998–2008
Evans RM, Mangelsdorf DJ (2014) Nuclear receptors, RXR, and the Big Bang. Cell 157:255–266
Fu ZQ, Yan S, Saleh A, Wang W, Ruble J, Oka N, Mohan R, Spoel SH, Tada Y, Zheng N, Dong X (2012) NPR3 and NPR4 are receptors for the immune signal salicylic acid in plants. Nature 486:228–232
Gomez-Roldan V, Fermas S, Brewer PB, Puech-Pages V, Dun EA, Pillot JP, Letisse F, Matusova R, Danoun S, Portais JC, Bouwmeester H, Bécard G, Beveridge CA, Rameau C, Rochange SF (2008) Strigolactone inhibition of shoot branching. Nature 455:189–194
Grienenberger E, Fletcher JC (2015) Polypeptide signaling molecules in plant development. Curr Opin Plant Biol 23:8–14
Kato M, Mizuno T, Shimizu T, Hakoshima T (1997) Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB. Cell 88:717–723
Melcher K, Ng LM, Zhou XE, Soon FF, Xu Y, Suino-Powell KM, Park SY, Weiner JJ, Fujii H, Chinnusamy V, Kovach A, Li J, Wang Y, Li J, Peterson FC, Jensen DR, Yong EL, Volkman BF, Cutler SR, Zhu JK, Xu HE (2009) A gate-latch-lock mechanism for hormone signalling by abscisic acid receptors. Nature 462:602–608
Murase K, Hirano Y, Sun TP, Hakoshima T (2008) Gibberellin-induced DELLA recognition by the gibberellin receptor GID1. Nature 456:459–463
Renaud JP, Rochel N, Ruff M, Vivat V, Chambon P, Gronemeyer H, Moras D (1995) Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid. Nature 378:681–689
Tan X, Calderon-Villalobos LI, Sharon M, Zheng C, Robinson CV, Estelle M, Zheng N (2007) Mechanism of auxin perception by the TIR1 ubiquitin ligase. Nature 446:640–645
Umehara M, Hanada A, Yoshida S, Akiyama K, Arite T, Takeda-Kamiya N, Magome H, Kamiya Y, Shirasu K, Yoneyama K, Kyozuka J, Yamaguchi S (2008) Inhibition of shoot branching by new terpenoid plant hormones. Nature 455:195–200
Wu Y, Zhang D, Chu JY, Boyle P, Wang Y, Brindle ID, De Luca V, Després C (2012) The Arabidopsis NPR1 protein is a receptor for the plant defense hormone salicylic acid. Cell Rep 1:639–647
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2018 Springer International Publishing AG, part of Springer Nature
About this chapter
Cite this chapter
Hakoshima, T. (2018). Overview of Proteins in Plant Hormone Signaling. In: Hejátko, J., Hakoshima, T. (eds) Plant Structural Biology: Hormonal Regulations. Springer, Cham. https://doi.org/10.1007/978-3-319-91352-0_1
Download citation
DOI: https://doi.org/10.1007/978-3-319-91352-0_1
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-319-91351-3
Online ISBN: 978-3-319-91352-0
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)