
DOI . ORG {
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Title[redir]:
F-actin dismantling through a redox-driven synergy between Mical and cofilin | Nature Cell Biology
Description:
Numerous cellular functions depend on actin filament (F-actin) disassembly. The best-characterized disassembly proteins, the ADF (actin-depolymerizing factor)/cofilins (encoded by the twinstar gene in Drosophila), sever filaments and recycle monomers to promote actin assembly. Cofilin is also a relatively weak actin disassembler, posing questions about mechanisms of cellular F-actin destabilization. Here we uncover a key link to targeted F-actin disassembly by finding that F-actin is efficiently dismantled through a post-translational-mediated synergism between cofilin and the actin-oxidizing enzyme Mical. We find that Mical-mediated oxidation of actin improves cofilin binding to filaments, where their combined effect dramatically accelerates F-actin disassembly compared with either effector alone. This synergism is also necessary and sufficient for F-actin disassembly in vivo, magnifying the effects of both Mical and cofilin on cellular remodelling, axon guidance and Semaphorin–Plexin repulsion. Mical and cofilin, therefore, form a redox-dependent synergistic pair that promotes F-actin instability by rapidly dismantling F-actin and generating post-translationally modified actin that has altered assembly properties. Grintsevich et al. discover that the redox enzyme Mical oxidizes F-actin to promote binding of the F-actin-severing protein cofilin, and that the synergy of Mical and cofilin is necessary and sufficient for F-actin disassembly in Drosophila.
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Keywords {🔍}
actin, cofilin, article, google, scholar, cas, mical, factin, cell, supplementary, severing, fig, micaloxidized, filaments, biol, nature, oxidation, copolymer, conditions, disassembly, red, drosophila, unoxidized, data, terman, note, time, nadph, subtilisin, experiments, oxactin, shown, binding, met, boxes, mol, nat, skeletal, yeast, presence, antibody, residue, fluorescence, compared, axon, access, cytoskeleton, human, independent, enhanced,
Topics {✒️}
nature portfolio semaphorin/plexin-mediated f-actin/cellular remodeling permissions reprints mical-oxidized anp-cross-linked f-actin privacy policy hem-derived cajal-retzius cells mical-oxidized cross-linked f-actin advertising open circles cross-linked q41c f-actin semaphorin/plexin/mical-dependent effects q41c f-actin cross-linking nature 463 nature yeast cofilin-kck-cy5-maleimide social media plexin-mediated axonal repulsion ox-actin—mical-oxidized g-actin 2d [upper middle 2d [lower middle rabbit skeletal actin-alexa488se cofilin-mediated f-actin severing cellular f-actin destabilization post-translational-mediated synergism redox-dependent synergistic pair q41c actin cross-linking promotes f-actin instability inducing f-actin disassembly1 actin-oxidizing enzyme mical rapidly dismantling f-actin reverses mical-mediated oxidation regulate f-actin disassembly targeted f-actin disassembly modulating f-actin disassembly impair f-actin assembly regulate f-actin dynamics f-actin disassembly factor q41c-xl f-actin wild-type met44 antibodies mical-oxidized f-actin semaphorin–plexin repulsion characterized mical-oxidized actin purified mical-oxidized actin semaphorin-dependent manner7 drosophila ovary development anp-modified actin skeletal f-actin curved drosophila bristle ruei-jiun hung & jonathan permissions
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headline:F-actin dismantling through a redox-driven synergy between Mical and cofilin
description:Numerous cellular functions depend on actin filament (F-actin) disassembly. The best-characterized disassembly proteins, the ADF (actin-depolymerizing factor)/cofilins (encoded by the twinstar gene in Drosophila), sever filaments and recycle monomers to promote actin assembly. Cofilin is also a relatively weak actin disassembler, posing questions about mechanisms of cellular F-actin destabilization. Here we uncover a key link to targeted F-actin disassembly by finding that F-actin is efficiently dismantled through a post-translational-mediated synergism between cofilin and the actin-oxidizing enzyme Mical. We find that Mical-mediated oxidation of actin improves cofilin binding to filaments, where their combined effect dramatically accelerates F-actin disassembly compared with either effector alone. This synergism is also necessary and sufficient for F-actin disassembly in vivo, magnifying the effects of both Mical and cofilin on cellular remodelling, axon guidance and SemaphorinâPlexin repulsion. Mical and cofilin, therefore, form a redox-dependent synergistic pair that promotes F-actin instability by rapidly dismantling F-actin and generating post-translationally modified actin that has altered assembly properties. Grintsevich et al. discover that the redox enzyme Mical oxidizes F-actin to promote binding of the F-actin-severing protein cofilin, and that the synergy of Mical and cofilin is necessary and sufficient for F-actin disassembly in Drosophila.
datePublished:2016-07-25T00:00:00Z
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Post-translational modifications
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headline:F-actin dismantling through a redox-driven synergy between Mical and cofilin
description:Numerous cellular functions depend on actin filament (F-actin) disassembly. The best-characterized disassembly proteins, the ADF (actin-depolymerizing factor)/cofilins (encoded by the twinstar gene in Drosophila), sever filaments and recycle monomers to promote actin assembly. Cofilin is also a relatively weak actin disassembler, posing questions about mechanisms of cellular F-actin destabilization. Here we uncover a key link to targeted F-actin disassembly by finding that F-actin is efficiently dismantled through a post-translational-mediated synergism between cofilin and the actin-oxidizing enzyme Mical. We find that Mical-mediated oxidation of actin improves cofilin binding to filaments, where their combined effect dramatically accelerates F-actin disassembly compared with either effector alone. This synergism is also necessary and sufficient for F-actin disassembly in vivo, magnifying the effects of both Mical and cofilin on cellular remodelling, axon guidance and SemaphorinâPlexin repulsion. Mical and cofilin, therefore, form a redox-dependent synergistic pair that promotes F-actin instability by rapidly dismantling F-actin and generating post-translationally modified actin that has altered assembly properties. Grintsevich et al. discover that the redox enzyme Mical oxidizes F-actin to promote binding of the F-actin-severing protein cofilin, and that the synergy of Mical and cofilin is necessary and sufficient for F-actin disassembly in Drosophila.
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Actin
Post-translational modifications
Life Sciences
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Cell Biology
Cancer Research
Developmental Biology
Stem Cells
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