Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization

@article{Yang1998CofilinPB,
  title={Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization},
  author={Neng Yang and Osamu Higuchi and Kazumasa Ohashi and Kyoko Nagata and Atsushi Wada and Kenji Kangawa and Eisuke Nishida and Kensaku Mizuno},
  journal={Nature},
  year={1998},
  volume={393},
  pages={809-812}
}
Rac is a small GTPase of the Rho family that mediates stimulus-induced actin cytoskeletal reorganization to generate lamellipodia. Little is known about the signalling pathways that link Rac activation to changes in actin filament dynamics. Cofilin is known to be a potent regulator of actin filament dynamics, and its ability to bind and depolymerize actin is abolished by phosphorylation of serine residue at 3 (refs 11, 12); however, the kinases responsible for this phosphorylation have not been… 
Cofilin Phosphorylation and Actin Cytoskeletal Dynamics Regulated by Rho- and Cdc42-Activated Lim-Kinase 2
TLDR
The results indicate that LIMK2 plays a crucial role both in Rho- and Cdc42-induced actin cytoskeletal reorganization, at least in part by inhibiting the functions of cofilin.
Lim kinases, regulators of actin dynamics.
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p57Kip2 Regulates Actin Dynamics by Binding and Translocating LIM-kinase 1 to the Nucleus*
TLDR
It is demonstrated that p57 regulates actin dynamics by binding and translocating LIMK-1 from the cytoplasm into the nucleus, which in turn results in a reorganization of actin fiber.
Phosphorylation of the cytoskeletal protein CAP1 controls its association with cofilin and actin
TLDR
The results suggest that S307 and S309 function in tandem; neither the alterations in binding cofilin and/or actin, nor the defects in rescuing the phenotype of the enlarged cell size in CAP1 knockdown cells was observed in point mutants of either S307 or S309.
Mitosis-dependent phosphorylation and activation of LIM-kinase 1.
TLDR
It is suggested that LIMK1 may play an important role in the cell cycle progression through regulation of actin cytoskeletal rearrangements through phosphorylation of cofilin.
Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation.
TLDR
The results suggest that TESK1 functions downstream of integrins and plays a key role in integrin-mediated actin reorganization, presumably through phosphorylating and inactivating cofilin.
LIM Kinase 1 Coordinates Microtubule Stability and Actin Polymerization in Human Endothelial Cells*
TLDR
The findings indicate that LIMK1 may coordinate microtubules and actin cytoskeleton in endothelial cells and thrombin-induced modulation of microtubule destabilization andActin polymerization.
Suppression of cofilin phosphorylation in insulin-stimulated ruffling membrane formation in KB cells.
TLDR
The results suggest that the examination of the kinetics and spatial regulation of phosphorylation is critical for the elucidation of the role of cofilin and upstream kinases in actin reorganization.
A Drosophila homolog of LIM-kinase phosphorylates cofilin and induces actin cytoskeletal reorganization.
TLDR
Observations suggest that the LIMK-cofilin signaling pathway for regulating actin filament dynamics is evolutionarily conserved between Drosophila and mammals.
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References

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TLDR
Cofilin was found to inhibit the superprecipitation of actin-myosin mixtures as well as the act in-activated myosin ATPase and the nucleation assay suggested that cofilin shortens the actin filaments and hence increases the filament number.
Control of actin dynamics in cell motility.
Actin polymerization plays a major role in cell movement. The controls of actin sequestration/desequestration and of filament turnover are two important features of cell motility. Actin binding
Molecular Characterization of abLIM, a Novel Actin-binding and Double Zinc Finger Protein
TLDR
It is speculated that abLIM may play a general role in bridging the actin-based cytoskeleton with an array of potential LIM protein-binding partners, which could mediate such interactions between actin filaments and cytoplasmic targets.
Reactivation of Phosphorylated Actin Depolymerizing Factor and Identification of the Regulatory Site (*)
TLDR
Alkaline phosphatase treatment of one Asp-N peptide converted it to a peptide of mass 673, demonstrating that this peptide contains the phosphate group, confirming that Ser3 in the encoded ADF is the single in vivo regulatory site.
rac p21 is involved in insulin-induced membrane ruffling and rho p21 is involved in hepatocyte growth factor- and 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced membrane ruffling in KB cells.
TLDR
Results indicate that rac p21 and rho GDI are involved in insulin-induced membrane ruffling and that HGF- and phorbol ester-induced membranes rufflings are involvedIn KB cells, where insulin and hepatocyte growth factor induced morphologically different membrane ruffedlings in KB cells.
Rho GTPases and the actin cytoskeleton.
TLDR
Members of the Rho family of small guanosine triphosphatases have emerged as key regulators of the actin cytoskeleton, and through their interaction with multiple target proteins, they ensure coordinated control of other cellular activities such as gene transcription and adhesion.
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