ArticleeLife2015
C-terminal threonines and serines play distinct roles in the desensitization of rhodopsin, a G protein-coupled receptor.
Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 79 citations in OpenAlex.
- Apusomonad rhodopsins: A new family of ultraviolet to blue light-absorbing rhodopsin channels.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- GPCR kinases phosphorylate GPCR C-terminal peptides in a hierarchical manner.Communications biology · 2025Article
- Systematic Assessment of Protein C-Termini Mutated in Human Disorders.Biomolecules · 2023Article
- Solo vs. Chorus: Monomers and Oligomers of Arrestin Proteins.International journal of molecular sciences · 2022Review
- Receptor-Arrestin Interactions: The GPCR Perspective.Biomolecules · 2021Review
- Structures of the archaerhodopsin-3 transporter reveal that disordering of internal water networks underpins receptor sensitization.Nature communications · 2021Article
- Review
- Biased GPCR signaling: Possible mechanisms and inherent limitations.Pharmacology & therapeutics · 2020Review
- Article
- Targeting arrestin interactions with its partners for therapeutic purposes.Advances in protein chemistry and structural biology · 2020Review
- Isoelectric Focusing to Quantify Rhodopsin Phosphorylation in Mouse Retina.Bio-protocol · 2019Article
- Article
- Distinct G protein-coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation.Nature communications · 2019Article
- The structural basis of the arrestin binding to GPCRs.Molecular and cellular endocrinology · 2019Review
- Dephosphorylation by protein phosphatase 2A regulates visual pigment regeneration and the dark adaptation of mammalian photoreceptors.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors.Cell · 2017Article
- Separation of photoreceptor cell compartments in mouse retina for protein analysis.Molecular neurodegeneration · 2017Article
- Effect of Rhodopsin Phosphorylation on Dark Adaptation in Mouse Rods.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016Article
- Functional role of positively selected amino acid substitutions in mammalian rhodopsin evolution.Scientific reports · 2016Article
- Quantitative modeling of the molecular steps underlying shut-off of rhodopsin activity in rod phototransduction.Molecular vision · 2016Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 1 country.
Funding
Abstract
Rod photoreceptors generate measurable responses to single-photon activation of individual molecules of the G protein-coupled receptor (GPCR), rhodopsin. Timely rhodopsin desensitization depends on phosphorylation and arrestin binding, which quenches G protein activation. Rhodopsin phosphorylation has been measured biochemically at C-terminal serine residues, suggesting that these residues are critical for producing fast, low-noise responses. The role of native threonine residues is unclear. We compared single-photon responses from rhodopsin lacking native serine or threonine phosphorylation sites. Contrary to expectation, serine-only rhodopsin generated prolonged step-like single-photon responses that terminated abruptly and randomly, whereas threonine-only rhodopsin generated responses that were only modestly slower than normal. We show that the step-like responses of serine-only rhodopsin reflect slow and stochastic arrestin binding. Thus, threonine sites play a privileged role in promoting timely arrestin binding and rhodopsin desensitization. Similar coordination of phosphorylation and arrestin binding may more generally permit tight control of the duration of GPCR activity.
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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.