Structural Aspects of Multistep Phosphorelay-Mediated Signaling in Plants
Jazyk angličtina Země Anglie, Velká Británie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem, přehledy
PubMed
26633861
DOI
10.1016/j.molp.2015.11.008
PII: S1674-2052(15)00451-7
Knihovny.cz E-zdroje
- Klíčová slova
- histidine kinase, multistep phosphorelay, phosphotransfer protein, response regulator, structure,
- MeSH
- Arabidopsis MeSH
- cytokininy metabolismus MeSH
- ethyleny metabolismus MeSH
- rostlinné proteiny chemie metabolismus MeSH
- signální transdukce MeSH
- vztahy mezi strukturou a aktivitou MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- přehledy MeSH
- Názvy látek
- cytokininy MeSH
- ethylene MeSH Prohlížeč
- ethyleny MeSH
- rostlinné proteiny MeSH
The multistep phosphorelay (MSP) is a central signaling pathway in plants integrating a wide spectrum of hormonal and environmental inputs and controlling numerous developmental adaptations. For the thorough comprehension of the molecular mechanisms underlying the MSP-mediated signal recognition and transduction, the detailed structural characterization of individual members of the pathway is critical. In this review we describe and discuss the recently known crystal and nuclear magnetic resonance structures of proteins acting in MSP signaling in higher plants, focusing particularly on cytokinin and ethylene signaling in Arabidopsis thaliana. We discuss the range of functional aspects of available structural information including determination of ligand specificity, activation of the receptor via its autophosphorylation, and downstream signal transduction through the phosphorelay. We compare the plant structures with their bacterial counterparts and show that although the overall similarity is high, the differences in structural details are frequent and functionally important. Finally, we discuss emerging knowledge on molecular recognition mechanisms in the MSP, and mention the latest findings regarding structural determinants of signaling specificity in the Arabidopsis MSP that could serve as a general model of this pathway in all higher plants.
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