ArticleThe Journal of biological chemistry2012
Mechanism for targeting the A-kinase anchoring protein AKAP18δ to the membrane.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 24 citations in OpenAlex.
- Article
- Enhanced Site-Specific Fluorescent Labeling of Membrane Proteins Using Native Nanodiscs.Biomolecules · 2025Article
- Genomic Signatures of Adaptation to Stress Reveal Shared Evolutionary Trends Between Tetrahymena utriculariae and Its Algal Endosymbiont, Micractinium tetrahymenae.Molecular biology and evolution · 2025Article
- A-Kinase Anchoring Proteins in Cardiac Myocytes and Their Roles in Regulating Calcium Cycling.Cells · 2023Review
- AKAP18δ Anchors and Regulates CaMKII Activity at Phospholamban-SERCA2 and RYR.Circulation research · 2022Article
- ScatteringNanoscale advances · 2021Article
- Native-like membrane models of E. coli polar lipid extract shed light on the importance of lipid composition complexity.BMC biology · 2021Article
- Lateral heterogeneity and domain formation in cellular membranes.Chemistry and physics of lipids · 2020Article
- PRDM9 forms a trimer by interactions within the zinc finger array.Life science alliance · 2019Article
- Quantification of Water Flux in Vesicular Systems.Scientific reports · 2018Article
- Application of Peak Intensity Analysis to Measurements of Protein Binding to Lipid Vesicles and Erythrocytes Using Fluorescence Correlation Spectroscopy: Dependence on Particle Size.The Journal of membrane biology · 2017Article
- Undulations Drive Domain Registration from the Two Membrane Leaflets.Biophysical journal · 2017Article
- The A-Kinase Anchoring Protein (AKAP) Glycogen Synthase Kinase 3β Interaction Protein (GSKIP) Regulates β-Catenin through Its Interactions with Both Protein Kinase A (PKA) and GSK3β.The Journal of biological chemistry · 2016Article
- AKAP18:PKA-RIIα structure reveals crucial anchor points for recognition of regulatory subunits of PKA.The Biochemical journal · 2016Article
- BK channel-mediated relaxation of urinary bladder smooth muscle: a novel paradigm for phosphodiesterase type 4 regulation of bladder function.The Journal of pharmacology and experimental therapeutics · 2014Article
- Local partition coefficients govern solute permeability of cholesterol-containing membranes.Biophysical journal · 2013Article
- Small-molecule screening identifies modulators of aquaporin-2 trafficking.Journal of the American Society of Nephrology : JASN · 2013Article
- Electrostatically induced recruitment of membrane peptides into clusters requires ligand binding at both interfaces.PloS one · 2012Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A-kinase anchoring proteins (AKAPs) are a family of scaffolding proteins that target PKA and other signaling molecules to cellular compartments and thereby spatiotemporally define cellular signaling events. The AKAP18 family comprises AKAP18α, AKAP18β, AKAP18γ, and AKAP18δ. The δ isoform targets PKA and phosphodiesterase PDE4D to AQP2 (aquaporin-2)-bearing vesicles to orchestrate the acute regulation of body water balance. Therefore, AKAP18δ must adopt a membrane localization that seems at odds with (i) its lack of palmitoylation or myristoylation sites that tailor its isoforms AKAP18α and AKAP18β to membrane compartments and (ii) the high sequence identity to the preferentially cytoplasmic AKAP18γ. Here, we show that the electrostatic attraction of the positively charged amino acids of AKAP18δ to negatively charged lipids explains its membrane targeting. As revealed by fluorescence correlation spectroscopy, the binding constant of purified AKAP18δ fragments to large unilamellar vesicles correlates (i) with the fraction of net negatively charged lipids in the bilayer and (ii) with the total amount of basic residues in the protein. Although distantly located on the sequence, these positively charged residues concentrate in the tertiary structure and form a clear binding surface. Thus, specific recruitment of the AKAP18δ-based signaling module to membranes such as those of AQP2-bearing vesicles must be achieved by additional mechanisms, most likely compartment-specific protein-protein interactions.
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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.