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Literature summary for 1.14.13.225 extracted from

  • Grintsevich, E.E.; Yesilyurt, H.G.; Rich, S.K.; Hung, R.J.; Terman, J.R.; Reisler, E.
    F-actin dismantling through a redox-driven synergy between Mical and cofilin (2016), Nat. Cell Biol., 18, 876-885.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
cofilin cofilin enhances Mical-mediated actin filament disassembly. Mical and cofilin synergize to drive Semaphorin-Plexin repulsive signalling and axon guidance Drosophila melanogaster
F-actin actin regulatory protein cofilin strongly suppresses the ability of F-actin to trigger Mical-mediated NADPH consumption Drosophila melanogaster

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster Q86BA1
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General Information

General Information Comment Organism
physiological function F-actin is efficiently dismantled through a post-translational-mediated synergism between cofilin and the actin-oxidizing enzyme Mical. 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 Drosophila melanogaster