Journal ArticleDOI
Putting a new twist on actin: ADF/cofilins modulate actin dynamics
TLDR
This review addresses aspects of ADF/cofilin structure, dynamics, regulation and function of this family of essential actin regulatory proteins.About:
This article is published in Trends in Cell Biology.The article was published on 1999-09-01. It has received 374 citations till now. The article focuses on the topics: Cofilin & Actin cytoskeleton.read more
Citations
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Journal ArticleDOI
Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase.
TL;DR: Results indicate that ROCK directly phosphorylates threonine 505 and activates LIMK2 downstream of RhoA and that this phosphorylation is essential for LimK2 to induce actin cytoskeletal reorganization.
Journal ArticleDOI
Signaling to the actin cytoskeleton in plants
TL;DR: This review focuses on five different cellular responses in which the actin cytoskeleton redistributes following extracellular stimulation: pollen tube tip growth and the self-incompatibility response; root hair responses to bacterial nodulation factors; light-mediated plastid positioning; nonhost resistance to fungal attack; and guard cell shape and turgor changes.
Journal ArticleDOI
Force activates smooth muscle α-actin promoter activity through the Rho signaling pathway
Xiao-Han Zhao,Carol Laschinger,Pam Arora,Katalin Szászi,Andras Kapus,Christopher A. McCulloch +5 more
TL;DR: Mechanical forces mediate actin assembly through the Rho–Rho-kinase–LIMK cofilin pathway, which promotes nuclear translocation of MRTF and subsequent activation of the SMA promoter to enhance SMA expression in fibroblasts.
Journal ArticleDOI
Actin filaments function as a tension sensor by tension-dependent binding of cofilin to the filament
TL;DR: In vitro, actin filament tension correlates with the binding and apparent activity of the filament-severing protein cofilin, suggesting a molecular mechanism by which cells respond to changes in mechanical force.
Journal ArticleDOI
Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation.
TL;DR: 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.
References
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Journal ArticleDOI
VMD: Visual molecular dynamics
TL;DR: VMD is a molecular graphics program designed for the display and analysis of molecular assemblies, in particular biopolymers such as proteins and nucleic acids, which can simultaneously display any number of structures using a wide variety of rendering styles and coloring methods.
Journal ArticleDOI
Atomic model of the actin filament
TL;DR: A unique orientation of the monomer with respect to the actin helix has been found and the main interactions are along the two-start helix with a contribution from a loop extending across the filament axis provided by the molecule in the adjacent strand.
Journal ArticleDOI
Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase
Silvia Arber,Freda A. Barbayannis,Hartwig Hanser,Corinna Schneider,Clement A. Stanyon,Ora Bernard,Pico Caroni +6 more
TL;DR: A mechanism for the regulation of cofilin and hence of actin dynamics in vivo is defined and should play a central role in regulating cell motility and morphogenesis by modulating the stability of act in cytoskeletal structures.
Journal ArticleDOI
Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization
Neng Yang,Osamu Higuchi,Kazumasa Ohashi,Kyoko Nagata,Atsushi Wada,Kenji Kangawa,Eisuke Nishida,Kensaku Mizuno,Kensaku Mizuno +8 more
TL;DR: It is shown that LIM-kinase 1 (LIMK-1), a serine/threonine kinase containing LIM and PDZ domains, phosphorylates cofilin at Ser’3, both in vitro and in vivo, which indicates that LIMK- 1 participates in Rac-mediated actin cytoskeletal reorganization, probably by phosphoryLating co Filin.
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Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia.
T.M. Svitkina,Gary G. Borisy +1 more
TL;DR: The leading edge of lamellipodia in Xenopus laevis keratocytes and fibroblasts was shown to have an extensively branched organization of actin filaments, which is supported by a dendritic brush, suggesting that ADF/cofilin, per se, is not sufficient for actin brush depolymerization and a regulatory step is required.