ArticleThe Journal of cell biology1987
Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding.
Article in The Journal of cell biology, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers, 1 of them a synthesis that pooled it.
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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.
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Who cites it
65 citing papers in PubMed, 1 synthesis or guideline pooled it, 192 citations in OpenAlex.
- Association of alpha-ADD1 Gene and Hypertension Risk: A Meta-Analysis.Medical science monitor : international medical journal of experimental and clinical research · 2015Pooled it
- Identification of a novel role for dematin in regulating red cell membrane function by modulating spectrin-actin interaction.The Journal of biological chemistry · 2012Trial
- Alpha-adducin Gly460Trp polymorphism and essential hypertension in Korea.Journal of Korean medical science · 2004Trial
- Dynein-driven regulation of postsynaptic membrane architecture and synaptic function.Journal of cell science · 2025Article
- Lack of adducin impairs the stability of endothelial adherens and tight junctions and may be required for cAMP-Rac1-mediated endothelial barrier stabilization.Scientific reports · 2022Article
- Variants in ADD1 cause intellectual disability, corpus callosum dysgenesis, and ventriculomegaly in humans.Genetics in medicine : official journal of the American College of Medical Genetics · 2022Article
- Novel candidate genes in esophageal atresia/tracheoesophageal fistula identified by exome sequencing.European journal of human genetics : EJHG · 2021Article
- Epithelial-specific isoforms of protein 4.1R promote adherens junction assembly in maturing epithelia.The Journal of biological chemistry · 2020Article
- The Spectrinome: The Interactome of a Scaffold Protein Creating Nuclear and Cytoplasmic Connectivity and Function.Experimental biology and medicine (Maywood, N.J.) · 2019Review
- Phosphorylation of adducin-1 by cyclin-dependent kinase 5 is important for epidermal growth factor-induced cell migration.Scientific reports · 2019Article
- Adducins inhibit lung cancer cell migration through mechanisms involving regulation of cell-matrix adhesion and cadherin-11 expression.Biochimica et biophysica acta. Molecular cell research · 2019Article
- Do Skeletal Dynamics Mediate Sugar Uptake and Transport in Human Erythrocytes?Biophysical journal · 2018Article
- A Review on Adducin from Functional to Pathological Mechanisms: Future Direction in Cancer.BioMed research international · 2018Review
- Adducin in tumorigenesis and metastasis.Oncotarget · 2017Review
- Feisty filaments: actin dynamics in the red blood cell membrane skeleton.Current opinion in hematology · 2016Review
- Article
- Fimbrin phosphorylation by metaphase Cdk1 regulates actin cable dynamics in budding yeast.Nature communications · 2016Article
- Spectrin's chimeric E2/E3 enzymatic activity.Experimental biology and medicine (Maywood, N.J.) · 2015Review
- Adducin-1 is essential for mitotic spindle assembly through its interaction with myosin-X.The Journal of cell biology · 2014Article
- There is more than one way to model an elephant. Experiment-driven modeling of the actin cytoskeleton.Biophysical journal · 2013Review
5 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Adducin is an erythrocyte membrane skeletal phosphoprotein comprised of two related subunits of 105,000 and 100,000 Mr. These peptides form a functional heterodimer, and the smaller of the two binds calmodulin in a calcium-dependent fashion. Although this protein has been physicochemically characterized, its function remains unknown. We have examined the interaction of human adducin with actin and with human erythrocyte spectrin using sedimentation, electrophoretic, and morphologic techniques. Purified adducin binds actin at physiologic ionic strength and bundles it into arrays of laterally arranged filaments, the adducin forming cross-bridges between the filaments at 35.2 /- 3.8 (2 SD) nm intervals. The stoichiometry of high affinity adducin binding to actin at saturation is 1:7, corresponding to a dimer of adducin for every actin helical unit. Adducin also promotes the binding of spectrin to actin independently of protein 4.1. At saturation, each adducin promotes the association of one spectrin heterodimer. The formation of this ternary spectrin-actin-adducin complex is independent of the assembly path, and the complex exists in a readily reversible equilibrium with the free components. The binding of adducin to actin and its ability to stimulate spectrin-actin binding is down-regulated by calmodulin in a calcium-dependent fashion. These results thus identify a putative role for adducin, and define a calcium- and calmodulin-dependent mechanism whereby higher states of actin association and its interaction with spectrin in the erythrocyte may be controlled.
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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.