ArticleThe Journal of biological chemistry2010
Global consequences of activation loop phosphorylation on protein kinase A.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 82 citations in OpenAlex.
- Protective Effect of Calcitonin Gene-Related Peptide on Corneal Epithelial Barrier in Experimental Dry Eye Models.Investigative ophthalmology & visual science · 2026Article
- A conserved phospho-switch controls receptor kinase SDS2 activation and homeostasis in rice immunity.Science advances · 2026Article
- Active zone plasticity couples sleep need to presynaptic hypophosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Mechanism of MEK1 activation by phosphorylation.Biophysical journal · 2026Article
- Activation loop phosphorylation and cGMP saturation of PKG regulate egress of malaria parasites.PLoS pathogens · 2024Article
- Article
- The "violin model": Looking at community networks for dynamic allostery.The Journal of chemical physics · 2023Review
- Conservation of land plant-specific receptor-like cytoplasmic kinase subfamily XI possessing a unique kinase insert domain.Frontiers in plant science · 2023Article
- Phosphorylation of enteroviral 2AJournal of medical virology · 2023Article
- Interaction of TOR and PKA Signaling inBiomolecules · 2022Review
- The 3-phosphoinositide-dependent protein kinase 1 is an essential upstream activator of protein kinase A in malaria parasites.PLoS biology · 2021Article
- 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
- A tripartite cooperative mechanism confers resistance of the protein kinase A catalytic subunit to dephosphorylation.The Journal of biological chemistry · 2020Article
- Activation of RSK by phosphomimetic substitution in the activation loop is prevented by structural constraints.Scientific reports · 2020Article
- Comprehensive Characterization of the Recombinant Catalytic Subunit of cAMP-Dependent Protein Kinase by Top-Down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019Article
- Understanding allosteric interactions in hMLKL protein that modulate necroptosis and its inhibition.Scientific reports · 2019Article
- How Electrostatic Coupling Enables Conformational Plasticity in a Tyrosine Kinase.Journal of the American Chemical Society · 2019Article
- Autophosphorylation activates c-Src kinase through global structural rearrangements.The Journal of biological chemistry · 2019Article
- Dynamic allostery-based molecular workings of kinase:peptide complexes.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Evolution of a dynamic molecular switch.IUBMB life · 2019Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Phosphorylation of the activation loop is one of the most common mechanisms for regulating protein kinase activity. The catalytic subunit of cAMP-dependent protein kinase autophosphorylates Thr(197) in the activation loop when expressed in Escherichia coli. Although mutation of Arg(194) to Ala prevents autophosphorylation, phosphorylation of Thr(197) can still be achieved by a heterologous protein kinase, phosphoinositide-dependent protein kinase (PDK1), in vitro. In this study, we examined the structural and functional consequences of adding a single phosphate to the activation loop of cAMP-dependent protein kinase by comparing the wild type C-subunit to the R194A mutant either in the presence or the absence of activation loop phosphorylation. Phosphorylation of Thr(197) decreased the K(m) by approximately 15- and 7-fold for kemptide and ATP, respectively, increased the stability of the enzyme as measured by fluorescence and circular dichroism, and enhanced the binding between the C-subunit and IP20, a protein kinase inhibitor peptide. Additionally, deuterium exchange coupled to mass spectrometry was used to compare the structural dynamics of these proteins. All of the regions of the C-subunit analyzed underwent amide hydrogen exchange at a higher or equal rate in the unphosphorylated enzyme compared with the phosphorylated enzyme. The largest changes occurred at the C terminus of the activation segment in the p + 1 loop/APE regions and the alphaH-alphaI loop motifs and leads to the prediction of a coordinated phosphorylation-induced salt bridge between two conserved residues, Glu(208) and Arg(280).
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.