ArticleBiophysical journal1998
Ca2+ regulation of gelsolin activity: binding and severing of F-actin.
Article in Biophysical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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.
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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
27 citing papers in PubMed, 86 citations in OpenAlex.
- Aspects of plant intelligence (ii).Plant signaling & behavior · 2026Review
- What about the Cytoskeletal and Related Proteins of Tapeworms in the Host's Immune Response? An Integrative Overview.Pathogens (Basel, Switzerland) · 2023Review
- An Assassin's Secret: Multifunctional Cytotoxic Compounds in the Predation Venom of the Assassin BugToxins · 2023Article
- The p53 and Calcium Regulated Actin Rearrangement in Model Cells.International journal of molecular sciences · 2022Article
- The actin polymerization factor Diaphanous and the actin severing protein Flightless I collaborate to regulate sarcomere size.Developmental biology · 2021Article
- The Activities of the Gelsolin Homology Domains of Flightless-I in Actin Dynamics.Frontiers in molecular biosciences · 2020Article
- Plastic Deformation and Fragmentation of Strained Actin Filaments.Biophysical journal · 2019Article
- Building and repairing the stereocilia cytoskeleton in mammalian auditory hair cells.Hearing research · 2019Review
- Polymerization and depolymerization of actin with nucleotide states at filament ends.Biophysical reviews · 2018Review
- Rapid cadmium SAD phasing at the standard wavelength (1 Å).Acta crystallographica. Section D, Structural biology · 2017Article
- Impaired Relaxation of Airway Smooth Muscle in Mice Lacking the Actin-Binding Protein Gelsolin.American journal of respiratory cell and molecular biology · 2017Article
- Article
- Regulation of the Postsynaptic Compartment of Excitatory Synapses by the Actin Cytoskeleton in Health and Its Disruption in Disease.Neural plasticity · 2016Review
- Activity and Ca²⁺ regulate the mobility of TRPV1 channels in the plasma membrane of sensory neurons.eLife · 2015Article
- Damage of hippocampal neurons in rats with chronic alcoholism.Neural regeneration research · 2014Article
- Cellular control of connective tissue matrix tension.Journal of cellular biochemistry · 2013Review
- Role and regulation of sperm gelsolin prior to fertilization.The Journal of biological chemistry · 2010Article
- Impact of actin filament stabilization on adult hippocampal and olfactory bulb neurogenesis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
- Drebrin a knockout eliminates the rapid form of homeostatic synaptic plasticity at excitatory synapses of intact adult cerebral cortex.The Journal of comparative neurology · 2009Article
- Lack of gelsolin promotes perpetuation of atrial fibrillation in the mouse heart.Journal of interventional cardiac electrophysiology : an international journal of arrhythmias and pacing · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Regulation of the F-actin severing activity of gelsolin by Ca2+ has been investigated under physiologic ionic conditions. Tryptophan fluorescence intensity measurements indicate that gelsolin contains at least two Ca2+ binding sites with affinities of 2.5 x 10(7) M-1 and 1.5 x 10(5) M-1. At F-actin and gelsolin concentrations in the range of those found intracellularly, gelsolin is able to bind F-actin with half-maximum binding at 0.14 microM free Ca2+ concentration. Steady-state measurements of gelsolin-induced actin depolymerization suggest that half-maximum depolymerization occurs at approximately 0.4 microM free Ca2+ concentration. Dynamic light scattering measurements of the translational diffusion coefficient for actin filaments and nucleated polymerization assays for number concentration of actin filaments both indicate that severing of F-actin occurs slowly at micromolar free Ca2+ concentrations. The data suggest that binding of Ca2+ to the gelsolin-F-actin complex is the rate-limiting step for F-actin severing by gelsolin; this Ca2+ binding event is a committed step that results in a Ca2+ ion bound at a high-affinity, EGTA-resistant site. The very high affinity of gelsolin for the barbed end of an actin filament drives the binding reaction equilibrium toward completion under conditions where the reaction rate is slow.
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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.