ArticleBiochemistry2011
Identification of in vitro autophosphorylation sites and effects of phosphorylation on the Arabidopsis CRINKLY4 (ACR4) receptor-like kinase intracellular domain: insights into conformation, oligomerization, and activity.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 25 citations in OpenAlex.
- Identification of critical functional residues of receptor-like kinase ERECTA.Journal of experimental botany · 2017Article
- Activation of the LRR Receptor-Like Kinase PSY1R Requires Transphosphorylation of Residues in the Activation Loop.Frontiers in plant science · 2017Article
- CLE peptide signaling and nitrogen interactions in plant root development.Plant molecular biology · 2016Review
- PP2A-3 interacts with ACR4 and regulates formative cell division in the Arabidopsis root.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Analysis of Phosphorylation of the Receptor-Like Protein Kinase HAESA during Arabidopsis Floral Abscission.PloS one · 2016Article
- Conserved phosphorylation sites in the activation loop of the Arabidopsis phytosulfokine receptor PSKR1 differentially affect kinase and receptor activity.The Biochemical journal · 2015Article
- Functional and phylogenetic characterization of proteins detected in various nematode intestinal compartments.Molecular & cellular proteomics : MCP · 2015Article
- A phylogenetic approach to study the origin and evolution of the CRINKLY4 family.Frontiers in plant science · 2015Article
- Article
- Mass spectrometry-based identification of native cardiac Nav1.5 channel α subunit phosphorylation sites.Journal of proteome research · 2012Article
- A neurosteroid analogue photolabeling reagent labels the colchicine-binding site on tubulin: a mass spectrometric analysis.Electrophoresis · 2012Article
- Deep amino acid sequencing of native brain GABAA receptors using high-resolution mass spectrometry.Molecular & cellular proteomics : MCP · 2012Article
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Authors and funding
4 authors at 2 institutions in 1 country.
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Abstract
Arabidopsis CRINKLY4 (ACR4) is a receptor-like kinase (RLK) that consists of an extracellular domain and an intracellular domain (ICD) with serine/threonine kinase activity. While genetic and cell biology experiments have demonstrated that ACR4 is important in cell fate specification and overall development of the plant, little is known about the biochemical properties of the kinase domain and the mechanisms that underlie the overall function of the receptor. To complement in planta studies of the function of ACR4, we have expressed the ICD in Escherichia coli as a soluble C-terminal fusion to the N-utilization substance A (NusA) protein, purified the recombinant protein, and characterized the enzymatic and conformational properties. The protein autophosphorylates via an intramolecular mechanism, prefers Mn(2+) over Mg(2+) as the divalent cation, and displays typical Michaelis-Menten kinetics with respect to ATP with an apparent K(m) of 6.67 ± 2.07 μM and a V(max) of 1.83 ± 0.18 nmol min(-1) mg(-1). Autophosphorylation is accompanied by a conformational change as demonstrated by circular dichroism, fluorescence spectroscopy, and limited proteolysis with trypsin. Analysis by nanoliquid chromatography and mass spectrometry revealed 16 confirmed sites of phosphorylation at Ser and Thr residues. Sedimentation velocity and gel filtration experiments indicate that the ICD has a propensity to oligomerize and that this property is lost upon autophosphorylation.
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