Key result
The combination of cofilin, coronin, and Aip1 disassembles actin filaments in a catastrophic mode by converting hypertwisted regions directly into monomers or short oligomers.
Why the study?
Coronin and Aip1 promote cofilin-mediated actin filament disassembly, but the mechanism is controversial, with conflicting reports of bursting versus severing alone.
The study demonstrates that cofilin, coronin, and Aip1 work together to cause catastrophic disassembly of actin filaments, rather than just enhanced severing.
Cofilin is an actin filament severing protein necessary for fast actin turnover dynamics. Coronin and Aip1 promote cofilin-mediated actin filament disassembly, but the mechanism is somewhat controversial. An early model proposed that the combination of cofilin, coronin, and Aip1 disassembled filaments in bursts. A subsequent study only reported severing. Here, we used EM to show that actin filaments convert directly into globular material. A monomer trap assay also shows that the combination of all three factors produces actin monomers faster than any two factors alone. We show that coronin accelerates the release of Pi from actin filaments and promotes highly cooperative cofilin binding to actin to create long stretches of polymer with a hypertwisted morphology. Aip1 attacks these hypertwisted regions along their sides, disintegrating them into monomers or short oligomers. The results are consistent with a catastrophic mode of disassembly, not enhanced severing alone.
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Tang et al. (2020) studied Actin filament dynamics. Cofilin, Aip1, and coronin was evaluated on Actin filament disassembly mechanism. The combination of cofilin, coronin, and Aip1 disassembles actin filaments in a catastrophic mode by converting hypertwisted regions directly into monomers or short oligomers.
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