ArticleThe Journal of biological chemistry2016
Structure of Guanylyl Cyclase Activator Protein 1 (GCAP1) Mutant V77E in a Ca2+-free/Mg2+-bound Activator State.
Article in The Journal of biological chemistry, 2016. 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, 26 citations in OpenAlex.
- NMR Structure of Retinal Guanylate Cyclase Activating Protein 5 (GCAP5) with R22A Mutation That Abolishes Dimerization and Enhances Cyclase Activation.Biochemistry · 2024Article
- Chemical shift assignments of retinal guanylyl cyclase activating protein 5 (GCAP5) with a mutation (R22A) that abolishes dimerization and enhances cyclase activation.Biomolecular NMR assignments · 2023Article
- NMR Structures of Calmodulin Bound to Two Separate Regulatory Sites in the Retinal Cyclic Nucleotide-Gated Channel.Biochemistry · 2022Article
- Structural basis of retinal membrane guanylate cyclase regulation by GCAP1 and RD3.Frontiers in molecular neuroscience · 2022Review
- NMR and EPR-DEER Structure of a Dimeric Guanylate Cyclase Activator Protein-5 from Zebrafish Photoreceptors.Biochemistry · 2021Article
- Regulation of retinal membrane guanylyl cyclase (RetGC) by negative calcium feedback and RD3 protein.Pflugers Archiv : European journal of physiology · 2021Review
- Structural Insights into Retinal Guanylate Cyclase Activator Proteins (GCAPs).International journal of molecular sciences · 2021Review
- Analysis of Arabidopsis TPK2 and KCO3 reveals structural properties required for KChannels (Austin, Tex.) · 2020Article
- Modulation of Guanylate Cyclase Activating Protein 1 (GCAP1) Dimeric Assembly by CaBiomolecules · 2020Article
- Molecular determinants of Guanylate Cyclase Activating Protein subcellular distribution in photoreceptor cells of the retina.Scientific reports · 2018Article
- Functional Status of Neuronal Calcium Sensor-1 Is Modulated by Zinc Binding.Frontiers in molecular neuroscience · 2018Article
- Dimerization of Neuronal Calcium Sensor Proteins.Frontiers in molecular neuroscience · 2018Review
- Article
- Structural Characterization of Ferrous Ion Binding to Retinal Guanylate Cyclase Activator Protein 5 from Zebrafish Photoreceptors.Biochemistry · 2017Article
- The Calcium-Dependent Switch Helix of L-Plastin Regulates Actin Bundling.Scientific reports · 2017Article
- Allosteric communication pathways routed by CaScientific reports · 2016Article
- Structure and Calcium Binding Properties of a Neuronal Calcium-Myristoyl Switch Protein, Visinin-Like Protein 3.PloS one · 2016Article
- Molecular properties of human guanylate cyclase-activating protein 2 (GCAP2) and its retinal dystrophy-associated variant G157R.The Journal of biological chemistryArticle
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
GCAP1, a member of the neuronal calcium sensor subclass of the calmodulin superfamily, confers Ca(2+)-sensitive activation of retinal guanylyl cyclase 1 (RetGC1). We present NMR resonance assignments, residual dipolar coupling data, functional analysis, and a structural model of GCAP1 mutant (GCAP1(V77E)) in the Ca(2+)-free/Mg(2+)-bound state. NMR chemical shifts and residual dipolar coupling data reveal Ca(2+)-dependent differences for residues 170-174. An NMR-derived model of GCAP1(V77E) contains Mg(2+) bound at EF2 and looks similar to Ca(2+) saturated GCAP1 (root mean square deviations = 2.0 Å). Ca(2+)-dependent structural differences occur in the fourth EF-hand (EF4) and adjacent helical region (residues 164-174 called the Ca(2+) switch helix). Ca(2+)-induced shortening of the Ca(2+) switch helix changes solvent accessibility of Thr-171 and Leu-174 that affects the domain interface. Although the Ca(2+) switch helix is not part of the RetGC1 binding site, insertion of an extra Gly residue between Ser-173 and Leu-174 as well as deletion of Arg-172, Ser-173, or Leu-174 all caused a decrease in Ca(2+) binding affinity and abolished RetGC1 activation. We conclude that Ca(2+)-dependent conformational changes in the Ca(2+) switch helix are important for activating RetGC1 and provide further support for a Ca(2+)-myristoyl tug mechanism.
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