ArticleJournal of molecular biology2006
Arrestin binding to calmodulin: a direct interaction between two ubiquitous signaling proteins.
Article in Journal of molecular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
What it found
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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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
50 citing papers in PubMed, 84 citations in OpenAlex.
- Mechanical mechanics-reclaiming a new battlefield for chronic liver disease.Journal of advanced research · 2026Review
- Arrestins as Possible Drug Targets.Biomolecules & therapeutics · 2025Review
- Molecular Insights into Diapause Mechanisms inInsects · 2025Article
- GPCR-dependent and -independent arrestin signaling.Trends in pharmacological sciences · 2024Review
- Arrestins: A Small Family of Multi-Functional Proteins.International journal of molecular sciences · 2024Review
- Expression of Untagged Arrestins in E. coli and Their Purification.Current protocols · 2023Article
- Short Arrestin-3-Derived Peptides Activate JNK3 in Cells.International journal of molecular sciences · 2022Article
- Structural evidence for visual arrestin priming via complexation of phosphoinositols.Structure (London, England : 1993) · 2022Article
- Novel and atypical pathways for serotonin signaling.Faculty reviews · 2021Review
- An arrestin-1 surface opposite of its interface with photoactivated rhodopsin engages with enolase-1.The Journal of biological chemistry · 2020Article
- β-Arrestin2 oligomers impair the clearance of pathological tau and increase tau aggregates.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Targeting arrestin interactions with its partners for therapeutic purposes.Advances in protein chemistry and structural biology · 2020Review
- Plethora of functions packed into 45 kDa arrestins: biological implications and possible therapeutic strategies.Cellular and molecular life sciences : CMLS · 2019Review
- The structural basis of the arrestin binding to GPCRs.Molecular and cellular endocrinology · 2019Review
- Arrestin mutations: Some cause diseases, others promise cure.Progress in molecular biology and translational science · 2019Review
- Scaffold Proteins: From Coordinating Signaling Pathways to Metabolic Regulation.Endocrinology · 2018Review
- Arrestins: Introducing Signaling Bias Into Multifunctional Proteins.Progress in molecular biology and translational science · 2018Review
- Therapeutic Targets for Treatment of Heart Failure: Focus on GRKs and β-Arrestins Affecting βAR Signaling.Frontiers in pharmacology · 2018Review
- The Diverse Roles of Arrestin Scaffolds in G Protein-Coupled Receptor Signaling.Pharmacological reviews · 2017Review
- A Comprehensive View of the β-Arrestinome.Frontiers in endocrinology · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Arrestins serve as multi-functional regulators of G-protein coupled receptors, interacting with hundreds of different receptor subtypes and a variety of other signaling proteins. Here we identify calmodulin as a novel arrestin interaction partner using three independent methods in vitro and in cells. Arrestin preferentially binds calcium-loaded calmodulin with a Kd value of approximately 7 microM, which is within range of endogenous calmodulin concentrations. The calmodulin binding site is localized on the concave side of the C-domain and a loop in the center of the arrestin molecule, significantly overlapping with receptor and microtubule-binding sites. Using purified proteins, we found that arrestins sequester calmodulin, preventing its binding to microtubules. Nanomolar affinity of arrestins for their cognate receptors makes calmodulin an ineffective competitor for arrestin binding at relatively high receptor concentrations. The arrestin-calmodulin interaction likely regulates the localization of both proteins and their availability for other interaction partners.
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What OpenQuestion holds
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.