ArticleThe Biochemical journal2015
Conserved phosphorylation sites in the activation loop of the Arabidopsis phytosulfokine receptor PSKR1 differentially affect kinase and receptor activity.
Article in The Biochemical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- A Water-Saving Drought Survival Phenotype in a Wheat TILLING Mutant Involves Survival-Biased Metabolic and Phosphorylation Reprogramming.Plant, cell & environment · 2026Article
- Betulinic Acid Delays Turnip Mosaic Virus Infection by Activating the Phytosulfokine Signalling Pathway in Nicotiana benthamiana.Molecular plant pathology · 2025Article
- The PP2CH- and PBL27-mediated phosphorylation switch of aluminium ion receptor PSKR1/ALR1 controls plant aluminum sensing ability.Nature plants · 2025Article
- Genome-Wide Characterization and Expression Profiling of Phytosulfokine Receptor Genes (Genes · 2024Article
- Moonlighting Crypto-Enzymes and Domains as Ancient and Versatile Signaling Devices.International journal of molecular sciences · 2024Review
- Ubiquitylation of PHYTOSULFOKINE RECEPTOR 1 modulates the defense response in tomato.Plant physiology · 2023Article
- Activation loop phosphorylation of a non-RD receptor kinase initiates plant innate immune signaling.Proceedings of the National Academy of Sciences of the United States of America · 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
- Genome-wide analysis and transcript profiling of PSKR gene family members in Oryza sativa.PloS one · 2020Article
- Sulfated plant peptide hormones.Journal of experimental botany · 2019Review
- Intramolecular crosstalk between catalytic activities of receptor kinases.Plant signaling & behavior · 2018Article
- Moonlighting Proteins and Their Role in the Control of Signaling Microenvironments, as Exemplified by cGMP and Phytosulfokine Receptor 1 (PSKR1).Frontiers in plant science · 2018Article
- Phosphorylation of the phytosulfokine peptide receptor PSKR1 controls receptor activity.Journal of experimental botany · 2017Article
- Identification of critical functional residues of receptor-like kinase ERECTA.Journal of experimental botany · 2017Article
- Insights into the Structure, Function, and Ion-Mediated Signaling Pathways Transduced by Plant Integrin-Linked Kinases.Frontiers in plant science · 2017Article
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
PSK (phytosulfokine) is a plant peptide hormone perceived by a leucine-rich repeat receptor kinase. Phosphosite mapping of epitope-tagged PSKR1 (phytosulfokine receptor 1) from Arabidopsis thaliana plants identified Ser(696) and Ser(698) in the JM (juxtamembrane) region and probably Ser(886) and/or Ser(893) in the AL (activation loop) as in planta phosphorylation sites. In vitro-expressed kinase was autophosphorylated at Ser(717) in the JM, and at Ser(733), Thr(752), Ser(783), Ser(864), Ser(911), Ser(958) and Thr(998) in the kinase domain. The LC-ESI-MS/MS spectra provided support that up to three sites (Thr(890), Ser(893) and Thr(894)) in the AL were likely to be phosphorylated in vitro. These sites are evolutionarily highly conserved in PSK receptors, indicative of a conserved function. Site-directed mutagenesis of the four conserved residues in the activation segment, Thr(890), Ser(893), Thr(894) and Thr(899), differentially altered kinase activity in vitro and growth-promoting activity in planta. The T899A and the quadruple-mutated TSTT-A (T890A/S893A/T894A/T899A) mutants were both kinase-inactive, but PSKR1(T899A) retained growth-promoting activity. The T890A and S893A/T894A substitutions diminished kinase activity and growth promotion. We hypothesize that phosphorylation within the AL activates kinase activity and receptor function in a gradual and distinctive manner that may be a means to modulate the PSK response.
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