ArticleBiochemistry2011
Robust self-association is a common feature of mammalian visual arrestin-1.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 56 citations in OpenAlex.
- Deceptive beauty of non-natural structures.Protein science : a publication of the Protein Society · 2026Review
- A key amino acid site associated with rhodopsin mammal evolution to diurnal vision.Scientific reports · 2025Article
- The Functional Role of Gate Loop Residues in Arrestin Binding to GPCRs.International journal of molecular sciences · 2025Article
- The role of arrestin-1 N-edge in rhodopsin binding.Cellular signalling · 2025Article
- Structure and self-association of Arrestin-1.Journal of structural biology · 2025Review
- Insights into the Activation and Self-Association of Arrestin-1.Biochemistry · 2025Article
- 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
- Do arrestin oligomers have specific functions?Cell signaling · 2023Article
- Article
- Solo vs. Chorus: Monomers and Oligomers of Arrestin Proteins.International journal of molecular sciences · 2022Review
- Structural evidence for visual arrestin priming via complexation of phosphoinositols.Structure (London, England : 1993) · 2022Article
- Functional compartmentalization of photoreceptor neurons.Pflugers Archiv : European journal of physiology · 2021Review
- An Eight Amino Acid Segment Controls Oligomerization and Preferred Conformation of the two Non-visual Arrestins.Journal of molecular biology · 2021Article
- Compartmentalization of Photoreceptor Sensory Cilia.Frontiers in cell and developmental biology · 2021Review
- Biological Role of Arrestin-1 Oligomerization.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020Article
- Targeting arrestin interactions with its partners for therapeutic purposes.Advances in protein chemistry and structural biology · 2020Review
- Arrestin-1 engineering facilitates complex stabilization with native rhodopsin.Scientific reports · 2019Article
- GPCRs and Signal Transducers: Interaction Stoichiometry.Trends in pharmacological sciences · 2018Review
- Molecular Defects of the Disease-Causing Human Arrestin-1 C147F Mutant.Investigative ophthalmology & visual science · 2018Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Arrestin-1 binds light-activated phosphorhodopsin and ensures rapid signal termination. Its deficiency in humans and mice results in prolonged signaling and rod degeneration. However, most of the biochemical studies were performed on bovine arrestin-1, which was shown to self-associate forming dimers and tetramers, although only the monomer binds rhodopsin. It is unclear whether self-association is a property of arrestin-1 in all mammals or a specific feature of bovine protein. To address this issue, we compared self-association parameters of purified human and mouse arrestin-1 with those of its bovine counterpart using multiangle light scattering. We found that mouse and human arrestin-1 also robustly self-associate, existing in a monomer-dimer-tetramer equilibrium. Interestingly, the combination of dimerization and tetramerization constants in these three species is strikingly different. While tetramerization of bovine arrestin-1 is highly cooperative (K(D,dim)(4) > K(D,tet)), K(D,dim) ∼ K(D,tet) in the mouse form and K(D,dim) ≪ K(D,tet) in the human form. Importantly, in all three species at very high physiological concentrations of arrestin-1 in rod photoreceptors, most of it is predicted to exist in oligomeric form, with a relatively low concentration of the free monomer. Thus, it appears that maintenance of low levels of the active monomer is the biological role of arrestin-1 self-association.
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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.