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Overview of Proteins in Plant Hormone Signaling

  • Toshio Hakoshima
Chapter

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.

References

  1. Cardozo T, Pagano MM (2004) The SCF Ubiquitin ligase: insights into a molecular machine. Nat Rev Mol Cell Biol 5:739–751CrossRefPubMedGoogle Scholar
  2. Chow B, McCourt P (2006) Plant hormone receptors: perception is everything. Genes Dev 20:1998–2008CrossRefPubMedGoogle Scholar
  3. Evans RM, Mangelsdorf DJ (2014) Nuclear receptors, RXR, and the Big Bang. Cell 157:255–266CrossRefPubMedPubMedCentralGoogle Scholar
  4. 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 486:228–232CrossRefPubMedPubMedCentralGoogle Scholar
  5. 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 455:189–194CrossRefPubMedGoogle Scholar
  6. Grienenberger E, Fletcher JC (2015) Polypeptide signaling molecules in plant development. Curr Opin Plant Biol 23:8–14CrossRefPubMedGoogle Scholar
  7. 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 88:717–723CrossRefPubMedGoogle Scholar
  8. 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 462:602–608CrossRefPubMedPubMedCentralGoogle Scholar
  9. Murase K, Hirano Y, Sun TP, Hakoshima T (2008) Gibberellin-induced DELLA recognition by the gibberellin receptor GID1. Nature 456:459–463CrossRefPubMedGoogle Scholar
  10. 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 378:681–689CrossRefPubMedGoogle Scholar
  11. 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 446:640–645CrossRefPubMedGoogle Scholar
  12. 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 455:195–200CrossRefPubMedGoogle Scholar
  13. 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 1:639–647CrossRefPubMedGoogle Scholar

Copyright information

© Springer International Publishing AG, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Structural Biology Laboratory, Nara Institute of Science and TechnologyIkomaJapan

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