ArticleFrontiers in molecular neuroscience2012
Synergetic effect of recoverin and calmodulin on regulation of rhodopsin kinase.
Article in Frontiers in molecular neuroscience, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Disulfide Dimerization of Neuronal Calcium Sensor-1: Implications for Zinc and Redox Signaling.International journal of molecular sciences · 2021Article
- Bringing the CaOpen biology · 2021Article
- Membrane Binding of Neuronal Calcium Sensor-1: Highly Specific Interaction with Phosphatidylinositol-3-Phosphate.Biomolecules · 2020Article
- Experimental Insight into the Structural and Functional Roles of the 'Black' and 'Gray' Clusters in Recoverin, a Calcium Binding Protein with Four EF-Hand Motifs.Molecules (Basel, Switzerland) · 2019Article
- Light-Induced Thiol Oxidation of Recoverin Affects Rhodopsin Desensitization.Frontiers in molecular neuroscience · 2018Article
- Functional Status of Neuronal Calcium Sensor-1 Is Modulated by Zinc Binding.Frontiers in molecular neuroscience · 2018Article
- Rational Design of Recombinant Papain-Like Cysteine Protease: Optimal Domain Structure and Expression Conditions for Wheat-Derived Enzyme Triticain-α.International journal of molecular sciences · 2017Article
- Plant-specific 4/1 polypeptide interacts with an endoplasmic reticulum protein related to human BAP31.Planta · 2017Article
- Protein and Signaling Networks in Vertebrate Photoreceptor Cells.Frontiers in molecular neuroscience · 2015Review
- A calcium-relay mechanism in vertebrate phototransduction.ACS chemical neuroscience · 2013Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphorylation of photoactivated rhodopsin by rhodopsin kinase (RK or GRK1), a first step of the phototransduction cascade turnoff, is under the control of Ca(2+)/recoverin. Here, we demonstrate that calmodulin, a ubiquitous Ca(2+)-sensor, can inhibit RK, though less effectively than recoverin does. We have utilized the surface plasmon resonance technology to map the calmodulin binding site in the RK molecule. Calmodulin does not interact with the recoverin-binding site within amino acid residues M1-S25 of the enzyme. Instead, the high affinity calmodulin binding site is localized within a stretch of amino acid residues V150-K175 in the N-terminal regulatory region of RK. Moreover, the inhibitory effect of calmodulin and recoverin on RK activity is synergetic, which is in agreement with the existence of separate binding sites for each Ca(2+)-sensing protein. The synergetic inhibition of RK by both Ca(2+)-sensors occurs over a broader range of Ca(2+)-concentration than by recoverin alone, indicating increased Ca(2+)-sensitivity of RK regulation in the presence of both Ca(2+)-sensors. Taken together, our data suggest that RK regulation by calmodulin in photoreceptor cells could complement the well-known inhibitory effect of recoverin on RK.
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