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Phosphorylation-dependent routing of RLP44 towards brassinosteroid or phytosulfokine signalling

Plants rely on cell surface receptors to integrate developmental and environmental cues into behaviour adapted to the conditions. The largest group of these receptors, leucine-rich repeat receptor-like kinases, form a complex interaction network that is modulated and extended by receptor-like protei...

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Hauptverfasser: Garnelo Gómez, Borja (Verfasst von) , Holzwart, Eleonore (Verfasst von) , Shi, Chaonan (Verfasst von) , Lozano-Durán, Rosa (Verfasst von) , Wolf, Sebastian (Verfasst von)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 20 October 2021
In: Journal of cell science
Year: 2021, Jahrgang: 134, Heft: 20, Pages: 1-13
ISSN:1477-9137
DOI:10.1242/jcs.259134
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1242/jcs.259134
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Verfasserangaben:Borja Garnelo Gómez, Eleonore Holzwart, Chaonan Shi, Rosa Lozano-Durán and Sebastian Wolf
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Zusammenfassung:Plants rely on cell surface receptors to integrate developmental and environmental cues into behaviour adapted to the conditions. The largest group of these receptors, leucine-rich repeat receptor-like kinases, form a complex interaction network that is modulated and extended by receptor-like proteins. This raises the question of how specific outputs can be generated when receptor proteins are engaged in a plethora of promiscuous interactions. RECEPTOR-LIKE PROTEIN 44 (RLP44) acts to promote both brassinosteroid and phytosulfokine signalling, which orchestrate diverse cellular responses. However, it is unclear how these activities are coordinated. Here, we show that RLP44 is phosphorylated in its highly conserved cytosolic tail and that this post-translational modification governs its subcellular localization. Whereas phosphorylation is essential for brassinosteroid-associated functions of RLP44, its role in phytosulfokine signalling is not affected by phospho-status. Detailed mutational analysis suggests that phospho-charge, rather than modification of individual amino acids determines routing of RLP44 to its target receptor complexes, providing a framework to understand how a common component of different receptor complexes can get specifically engaged in a particular signalling pathway.
Beschreibung:Gesehen am 04.12.2021
Beschreibung:Online Resource
ISSN:1477-9137
DOI:10.1242/jcs.259134

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