ArticleJournal of molecular biology2011
A myristoyl/phosphoserine switch controls cAMP-dependent protein kinase association to membranes.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Mussel Spermatozoa Express a Specific Isoform of the Catalytic Subunit of cAMP-Dependent Protein Kinase.Molecular reproduction and development · 2026Article
- Structural determinants of protein kinase A essential for CFTR channel activation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The structures of protein kinase A in complex with CFTR: Mechanisms of phosphorylation and noncatalytic activation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Post-translational modifications in the Protein Data Bank.Acta crystallographica. Section D, Structural biology · 2024Review
- PKA regulation of neuronal function requires the dissociation of catalytic subunits from regulatory subunits.bioRxiv : the preprint server for biology · 2024Article
- Inhibition of N-myristoyltransferase activity promotes androgen receptor degradation in prostate cancer.The Prostate · 2024Article
- Conformational regulation and target-myristoyl switch of calcineurin B homologous protein 3.eLife · 2023Article
- An NMR portrait of functional and dysfunctional allosteric cooperativity in cAMP-dependent protein kinase A.FEBS letters · 2023Review
- Novel Hits for N-Myristoyltransferase Inhibition Discovered by Docking-Based Screening.Molecules (Basel, Switzerland) · 2022Article
- A role of salt bridges in mediating drug potency: A lesson from the N-myristoyltransferase inhibitors.Frontiers in molecular biosciences · 2022Article
- Myristoylation alone is sufficient for PKA catalytic subunits to associate with the plasma membrane to regulate neuronal functions.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Smoothened transduces Hedgehog signals via activity-dependent sequestration of PKA catalytic subunits.PLoS biology · 2021Article
- Article
- Protein-N-myristoylation-dependent phosphorylation of serine 13 of tyrosine kinase Lyn by casein kinase 1γ at the Golgi during intracellular protein traffic.Scientific reports · 2020Article
- N-myristoylation: from cell biology to translational medicine.Acta pharmacologica Sinica · 2020Review
- A tripartite cooperative mechanism confers resistance of the protein kinase A catalytic subunit to dephosphorylation.The Journal of biological chemistry · 2020Article
- Kinase Atlas: Druggability Analysis of Potential Allosteric Sites in Kinases.Journal of medicinal chemistry · 2019Review
- STE20/PAKA Protein Kinase Gene Releases an Autoinhibitory Domain through Pre-mRNA Alternative Splicing in the DermatophyteInternational journal of molecular sciences · 2018Article
- Protein Lipidation: Occurrence, Mechanisms, Biological Functions, and Enabling Technologies.Chemical reviews · 2018Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The cAMP-dependent protein kinase [protein kinase A (PKA)] mediates a myriad of cellular signaling events, and its activity is tightly regulated in both space and time. Among these regulatory mechanisms is N-myristoylation, whose biological role has been elusive. Using a combination of thermodynamics, kinetics, and spectroscopic methods, we analyzed the effects of N-myristoylation and phosphorylation at Ser10 on the interactions of PKA with model membranes. We found that, in the absence of lipids, the myristoyl group is tucked into the hydrophobic binding pocket of the enzyme (myr-in state). Upon association with lipid bilayers, the myristoyl group is extruded and inserts into the hydrocarbon region of the lipid bilayer (myr-out state). NMR data indicate that the enzyme undergoes conformational equilibrium between myr-in and myr-out states, which can be shifted byeither interaction with membranes and/or phosphorylation at Ser10. Our results provide evidence that the membrane binding motif of the myristoylated C-subunit of PKA (PKA-C) steers the enzyme toward lipids independent of its regulatory subunit or an A-kinase anchoring protein, providing an additional mechanism to localize the enzyme near membrane-bound substrates.
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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.