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
Cellular Motility Driven by Assembly and Disassembly of Actin Filaments
Thomas D. Pollard,Gary G. Borisy +1 more
TL;DR: A core set of proteins including actin, Arp2/3 complex, profilin, capping protein, and ADF/cofilin can reconstitute the process in vitro, and mathematical models of the constituent reactions predict the rate of motion.
Journal ArticleDOI
Rho GTPases and their effector proteins.
Anne L. Bishop,Alan Hall +1 more
TL;DR: The main focus of this review will be Rho, Rac and Cdc42, the three best characterized mammalian Rho GTPases, though the genetic analysis of RhoGTPases in lower eukaryotes is making increasingly important contributions to this field.
Journal ArticleDOI
Molecular Mechanisms Controlling Actin Filament Dynamics in Nonmuscle Cells
TL;DR: How motile cells regulate actin filament assembly at their leading edge is reviewed, including how Arp2/3 complex is incorporated into the network, and new filaments are capped rapidly, so that activated Arp1/2 complex must be supplied continuously to keep the network growing.
Journal ArticleDOI
Astrocyte-Neuron Lactate Transport Is Required for Long-Term Memory Formation
Akinobu Suzuki,Sarah A. Stern,Ozlem Bozdagi,George W. Huntley,Ruth H. Walker,Pierre J. Magistretti,Cristina M. Alberini +6 more
TL;DR: It is concluded that astrocyte-neuron lactate transport is required for long-term memory formation, suggesting that lactate import into neurons is necessary for long -term memory.
Journal ArticleDOI
Actin Binding Proteins: Regulation of Cytoskeletal Microfilaments
C.G. dos Remedios,Deepak Chhabra,Murat Kekic,Irina Dedova,Masako Tsubakihara,Desiree A. Berry,Neil J. Nosworthy +6 more
TL;DR: Several ABPs that regulate actin-driven assembly, i.e., movement that is independent of motor proteins, are selected that represent a family of related proteins in nature and are widely distributed in nature.
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.
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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.
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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.