F-actin dismantling through a redox-driven synergy between Mical and cofilin
| Autor: | Shannon K. Rich, Hunkar Gizem Yesilyurt, Ruei-Jiun Hung, Emil Reisler, Jonathan R. Terman, Elena E. Grintsevich |
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| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
Cofilin 1
0301 basic medicine macromolecular substances Plasma protein binding Biology Medical and Health Sciences DNA-binding protein Article 03 medical and health sciences 0302 clinical medicine Animals Actin Effector Cell Biology Biological Sciences Cofilin Actin cytoskeleton Actins Cell biology DNA-Binding Proteins Actin Cytoskeleton Destrin Drosophila melanogaster 030104 developmental biology Generic health relevance Rabbits Oxidation-Reduction 030217 neurology & neurosurgery Developmental Biology Protein Binding |
| Zdroj: | Grintsevich, EE; Yesilyurt, HG; Rich, SK; Hung, R-J; Terman, JR; & Reisler, E. (2016). F-actin dismantling through a redox-driven synergy between Mical and cofilin. NATURE CELL BIOLOGY, 18(8), 876-+. doi: 10.1038/ncb3390. UCLA: Retrieved from: http://www.escholarship.org/uc/item/6kf5x7m4 Nature cell biology Nature cell biology, vol 18, iss 8 |
| Popis: | 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 invivo, 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. |
| Databáze: | OpenAIRE |
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