ArticleBiophysical journal1998
Severing of F-actin by the amino-terminal half of gelsolin suggests internal cooperativity in gelsolin.
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 24 papers.
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Who cites it
24 citing papers in PubMed.
- Mechanism of actin filament severing and capping by gelsolin.Nature structural & molecular biology · 2025Article
- Benefits and challenges of reconstituting the actin cortex.Cytoskeleton (Hoboken, N.J.) · 2024Review
- mTORC2 Loss in Oligodendrocyte Progenitor Cells Results in Regional Hypomyelination in the Central Nervous System.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023Article
- Long-Range and Directional Allostery of Actin Filaments Plays Important Roles in Various Cellular Activities.International journal of molecular sciences · 2020Review
- Novel inter-domain CaJournal of muscle research and cell motility · 2020Review
- The Activities of the Gelsolin Homology Domains of Flightless-I in Actin Dynamics.Frontiers in molecular biosciences · 2020Article
- Differential expression ofEXCLI journal · 2020Article
- Interaction Between a Gelsolin from Dendrorhynchus zhejiangensis with Three Gelsolin-Like Domains and Actin In Vitro.The protein journal · 2018Article
- Cholesterol-Dependent Phase-Demixing in Lipid Bilayers as a Switch for the Activity of the Phosphoinositide-Binding Cytoskeletal Protein Gelsolin.Biochemistry · 2016Article
- siRNA induces gelsolin gene transcription activation in human esophageal cancer cell.Scientific reports · 2015Article
- Gelsolin-Like Domain 3 Plays Vital Roles in Regulating the Activities of the Lily Villin/Gelsolin/Fragmin Superfamily.PloS one · 2015Article
- Global shapes of F-actin depolymerization-competent minimal gelsolins: insight into the role of g2-g3 linker in pH/Ca2+ insensitivity of the first half.The Journal of biological chemistry · 2013Article
- Gelsolin activity controls efficient early HIV-1 infection.Retrovirology · 2013Article
- Cerebrospinal fluid levels of Aβ42 relationship with cholinergic cortical activity in Alzheimer's disease patients.Journal of neural transmission (Vienna, Austria : 1996) · 2012Article
- Gelsolin and non-muscle myosin IIA interact to mediate calcium-regulated collagen phagocytosis.The Journal of biological chemistry · 2011Article
- Visual insight into how low pH alone can induce actin-severing ability in gelsolin under calcium-free conditions.The Journal of biological chemistry · 2011Article
- Conformational dynamics of actin: effectors and implications for biological function.Cytoskeleton (Hoboken, N.J.) · 2010Review
- Caenorhabditis elegans gelsolin-like protein 1 is a novel actin filament-severing protein with four gelsolin-like repeats.The Journal of biological chemistry · 2008Article
- RPEL motifs link the serum response factor cofactor MAL but not myocardin to Rho signaling via actin binding.Molecular and cellular biology · 2008Article
- Mini-thin filaments regulated by troponin-tropomyosin.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
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Authors and funding
7 authors.
Funding
Abstract
Gelsolin is a Ca2+-regulated actin-binding protein that can sever, cap, and nucleate growth from the pointed ends of actin filaments. In this study we have measured the binding of the amino-terminal half of gelsolin, G1-3, to pyrene-labeled F-actin as a function of Ca2+ concentration. The rate of binding is shown to be dependent on micromolar concentrations of Ca2+. Independent experiments demonstrate that conformational changes in G1-3 are induced by micromolar concentrations of Ca2+. Titrations of pyrene-F-actin with G1-3 and gelsolin show that the quenching of pyrene fluorescence is identical in extent and stoichiometry for both G1-3 and gelsolin. In contrast, severing of F-actin by G1-3 is found to be much less efficient than is severing by gelsolin. In experiments in which F-actin severing is quantitatively measured, the filament number is found to be proportional to the 1.35 power of the G1-3 concentration. This deviation from linearity may be explained by cooperativity; the binding of two G1-3 molecules in close proximity may lead to cooperative severing of the polymer, thus increasing the severing efficiency. This model is supported by experiments that show that the efficiency of G1-3 severing of F-actin increases with increasing G1-3:F-actin ratios. Extrapolating from these results, we conclude that G4-6, the carboxyl-terminal half of gelsolin, has an active role in the severing of F-actin by intact gelsolin. Whereas F-actin severing by G1-3 is enhanced by cooperative binding of two separate G1-3 molecules, cooperativity is inherent to intact gelsolin because the cooperative partners are covalently linked.
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