Cited by 172Cellular Mechanics and InteractionsProtein Kinase Regulation and GTPase SignalingCellular transport and secretion

Cofilin promotes stimulus-induced lamellipodium formation by generating an abundant supply of actin monomers

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Kiuchi, Tai, Ohashi, Kazumasa, Kurita, Souichi, Mizuno, Kensaku·2007·The Journal of Cell Biology

Abstract

Cofilin stimulates actin filament disassembly and accelerates actin filament turnover. Cofilin is also involved in stimulus-induced actin filament assembly during lamellipodium formation. However, it is not clear whether this occurs by replenishing the actin monomer pool, through filament disassembly, or by creating free barbed ends, through its severing activity. Using photoactivatable Dronpa-actin, we show that cofilin is involved in producing more than half of all cytoplasmic actin monomers and that the rate of actin monomer incorporation into the tip of the lamellipodium is dependent on the size of this actin monomer pool. Finally, in cofilin-depleted cells, stimulus-induced actin monomer incorporation at the cell periphery is attenuated, but the incorporation of microinjected actin monomers is not. We propose that cofilin contributes to stimulus-induced actin filament assembly and lamellipodium extension by supplying an abundant pool of cytoplasmic actin monomers.

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  • The diffusion of WT and S3A cofilin, but not S3E cofilin, in the resting state was significantly impeded by their binding to F-actins.

    “These findings suggest that the diffusion of WT or S3A cofilin, but not S3E cofilin, was significantly impeded by their binding to F-actins1326.”

    From State-dependent diffusion of actin-depolymerizing factor/cofilin underlies the enlargement and shrinkage of dendritic spines (2016) · cites this paper as [26]

    The Results section, “Cofilin inactivation or knockdown markedly decreases the cytoplasmic actin monomer pool” (page unavailable), measures diffusion of photoactivated Dp-actin while cofilin variants are expressed—not diffusion of the cofilin variants themselves. Searches for cofilin diffusion and F-actin binding found no passage establishing that WT and S3A cofilin, but not S3E, have impeded diffusion in resting cells. (LLM, conf=0.76)

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Cited by

Sorted by citations

Authors
Kiuchi, T., Ohashi, K., Kurita, S., & Mizuno, K.
Affiliations
Tohoku University (JP)
Corresponding author
Mizuno, Kensaku
Venue
The Journal of Cell Biology
Published
2007-04-30
Volume
177
Issue
3
Pages
465-476
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
OpenAlex
W2154744729
Cited by
172
References
1
Citations by year
2026: 2 · 2025: 2 · 2024: 4 · 2023: 6 · 2022: 2 · 2021: 9 · 2020: 2 · 2019: 2 · 2018: 6 · 2017: 4 · 2016: 10 · 2015: 12 · 2014: 13 · 2013: 16 · 2012: 11
FWCI
7.72
Type
journal article
Language
en
Open access
Licence
cc-by-nc-sa
Locations
  • The Journal of Cell Biology (publishedVersion)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords
cofilin, lamellipodium formation, actin monomer, actin filament disassembly, actin filament turnover, actin polymerization, barbed end, cell motility, actin filament severing
MeSH terms
Actins, Animals, Chlorocebus aethiops, Cytoplasm, Humans, Actin Cytoskeleton, Pseudopodia, COS Cells, Actin Depolymerizing Factors, Mice

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