ArticleJournal of experimental botany2017
Phosphorylation of the phytosulfokine peptide receptor PSKR1 controls receptor activity.
Article in Journal of experimental botany, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 29 citations in OpenAlex.
- A Phytosulfokine signaling module activates the Nod factor receptor to control soybean nodulation.Nature communications · 2026Article
- Crosstalk and reciprocal regulation of phosphorylation and ubiquitination mediated by receptor-like kinases and U-box E3 ligases during plant growth and environmental stress responses.Plant communications · 2026Review
- Molecular Regulators of In Vitro Regeneration in Wheat: Roles of Morphogenic Factors in Transformation, Genome Editing, and Breeding.International journal of molecular sciences · 2026Review
- Phosphovariants of the canonical heterotrimeric Gα protein, GPA1, differentially affect G protein activity and Arabidopsis development.bioRxiv : the preprint server for biology · 2026Article
- Betulinic Acid Delays Turnip Mosaic Virus Infection by Activating the Phytosulfokine Signalling Pathway in Nicotiana benthamiana.Molecular plant pathology · 2025Article
- Guanylate cyclase activity in moss: revisiting the role of ERECTA-like receptors.Physiology and molecular biology of plants : an international journal of functional plant biology · 2025Article
- The PP2CH- and PBL27-mediated phosphorylation switch of aluminium ion receptor PSKR1/ALR1 controls plant aluminum sensing ability.Nature plants · 2025Article
- Overexpression ofFrontiers in plant science · 2025Article
- A novel LRR receptor-like kinase BRAK reciprocally phosphorylates PSKR1 to enhance growth and defense in tomato.The EMBO journal · 2024Article
- Moonlighting Crypto-Enzymes and Domains as Ancient and Versatile Signaling Devices.International journal of molecular sciences · 2024Review
- Sulfated peptides and their receptors: Key regulators of plant development and stress adaptation.Plant communications · 2024Review
- Sulfated peptides: key players in plant development, growth, and stress responses.Frontiers in plant science · 2024Review
- Effects of drought and salt stress on the root phenotype of wheat seedlings and underlying gene expression analysis.Frontiers in plant science · 2024Article
- Ubiquitylation of PHYTOSULFOKINE RECEPTOR 1 modulates the defense response in tomato.Plant physiology · 2023Article
- Phytosulfokine peptides, their receptors, and functions.Frontiers in plant science · 2023Review
- (De)Activation (Ir)Reversibly or Degradation: Dynamics of Post-Translational Protein Modifications in Plants.Life (Basel, Switzerland) · 2022Review
- Proteomics and Interspecies Interaction Analysis Revealed Abscisic Acid Signalling to Be the Primary Driver for Oil Palm's Response against Red Palm Weevil Infestation.Plants (Basel, Switzerland) · 2021Article
- Tyrosylprotein sulfotransferase-dependent and -independent regulation of root development and signaling by PSK LRR receptor kinases in Arabidopsis.Journal of experimental botany · 2021Article
- Moonlighting Proteins Shine New Light on Molecular Signaling Niches.International journal of molecular sciences · 2021Review
- Paired Receptor and Coreceptor Kinases Perceive Extracellular Signals to Control Plant Development.Plant physiology · 2020Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The phytosulfokine peptide receptor PSKR1 is modified by phosphorylation of its cytoplasmic kinase domain. We analyzed defined phosphorylation sites by site-directed mutagenesis with regard to kinase activity in vitro and receptor activity in planta. S696 and S698 in the juxtamembrane (JM) domain are phosphorylated in planta. The phosphomimetic S696D/S698D replacements resulted in reduced transphosphorylation activity of PSKR1 kinase in vitro but did not reduce autophosphorylation activity. Growth-promoting activity of the PSKR1(S696D/S698D) receptor isoform was impaired in the shoot but not in the root. The JM domain thus seems to be important for phosphorylation of a target protein required for shoot growth promotion. The phosphomimetic replacement T998D at the C-terminus (CT) abolished kinase activity in vitro but not receptor function in planta, indicating that additional levels of regulation exist in planta. A possible mode of receptor regulation is the interaction with regulatory proteins such as the calcium sensor calmodulin (CaM). We show that the previously reported binding of CaM2 to PSKR1 is calcium-dependent, occurs predominately to the hypophosphorylated soluble PSKR1 kinase, and does not significantly change PSKR1 kinase activity. In conclusion, our results show that peptide signaling of growth by PSKR1 is regulated by differential phosphorylation of the juxtamembrane and C-terminal domains of the intracellular receptor part and suggest that interaction of PSKR1 with CaM serves a function other than the regulation of kinase activity.
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