ArticleBiochemistry2012
Substrate-induced changes in the dynamics of rhodopsin kinase (G protein-coupled receptor kinase 1).
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Revealing GRK5 Activation Features by Interpretable Machine Learning and Molecular Dynamics Simulation.International journal of molecular sciences · 2026Article
- Mechanisms of Rhodopsin-Related Inherited Retinal Degeneration and Pharmacological Treatment Strategies.Cells · 2025Review
- The Open Question of How GPCRs Interact with GPCR Kinases (GRKs).Biomolecules · 2021Article
- Phosphorylation at Serine 21 in G protein-coupled receptor kinase 1 (GRK1) is required for normal kinetics of dark adaption in rod but not cone photoreceptors.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Navigating the conformational landscape of G protein-coupled receptor kinases during allosteric activation.The Journal of biological chemistry · 2017Article
- Article
- Dynamic peptides of human TPP1 fulfill diverse functions in telomere maintenance.Nucleic acids research · 2016Article
- Protein and Signaling Networks in Vertebrate Photoreceptor Cells.Frontiers in molecular neuroscience · 2015Review
- Structural insights into G protein-coupled receptor kinase function.Current opinion in cell biology · 2014Review
- From atomic structures to neuronal functions of g protein-coupled receptors.Annual review of neuroscience · 2013Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
G protein-coupled receptor (GPCR) kinases (GRKs) instigate the desensitization of activated GPCRs via phosphorylation that promotes interaction with arrestins, thereby preventing the interaction of GPCRs with heterotrimeric G proteins. A current proposed model of GRK1 activation involves the binding of activated rhodopsin (Rho*) to the N-terminal region of GRK1. Perhaps concomitantly, this N-terminal region also stabilizes a closed, active conformation of the kinase domain. To further probe this model, we mapped changes in the backbone flexibility of GRK1 as it binds to its two substrates, adenosine triphosphate (Mg(2+)·ATP) and Rho*. We found that the conformational flexibility of GRK1 was reduced in the presence of either Mg(2+)·ATP or Rho*, with Mg(2+)·ATP having the greatest effect. In a truncated form of GRK1 lacking the N-terminal region (ΔN-GRK1), peptides that directly interact with ATP were not as dramatically stabilized by adding Mg(2+)·ATP, and dynamics were greater in the interface between the large lobe of the kinase domain and the regulator of the G protein signaling homology domain. In the presence of Mg(2+)·ATP, the influence of Rho* versus Rho on GRK1 dynamics was negligible.
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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.