The ADF/Cofilin Proteins: Stimulus-responsive Modulators of Actin Dynamics

Moon, Anne; Drubin, David G.

doi:10.1091/mbc.6.11.1423

Cited by 250 publications

(214 citation statements)

References 84 publications

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“…An N-terminal 180-amino acid fragment of Abplp binds to filamentous actin in vitro (Chamany and Drubin, unpublished results) and has sequence similarity to proteins of the ADF/cofilin family (reviewed in Moon and Drubin, 1995), Dictyostelium coactosin (de Hostos et al, 1993), and an N-terminal domain of the vertebrate neuronal actin-binding protein drebrin (23% amino acid identity with rat drebrin A over a 130-amino acid span; see MATERIALS AND METH-ODS). Cofilins can sever actin filaments while coactosin and drebrin do not; therefore, these evolutionarily related proteins clearly do not all function in a precisely analogous manner, but a common theme may lie in the roles of these proteins as stimulus-responsive Vol.…”

Section: Mutations In Rvs167 and Abp1 Show Similar Phenotypes And Genmentioning

confidence: 99%

“…8, February 1997 modulators of actin filament architecture and dynamics. A large body of evidence links changes in the activity of cofilin, for example, to cytoskeletal rearrangements which occur in response to receptor stimulation in cells such as platelets and T-cells (Moon and Drubin, 1995). Marked changes in the association of drebrin with cellular actin-containing structures accompanies the retinoic acid-induced differentiation of neuroblastoma cells (Asada et al, 1994), and expression of drebrin in non-neuronal cell types leads to the formation of neurite-like outgrowths (Shirao et al, 1992).…”

Section: Mutations In Rvs167 and Abp1 Show Similar Phenotypes And Genmentioning

confidence: 99%

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Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, an adenylyl cyclase-associated protein and the actin cytoskeleton.

Lila

Drubin

1997

MBoC

164

219

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Section: Mutations In Rvs167 and Abp1 Show Similar Phenotypes And Genmentioning

confidence: 99%

Section: Mutations In Rvs167 and Abp1 Show Similar Phenotypes And Genmentioning

confidence: 99%

Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, an adenylyl cyclase-associated protein and the actin cytoskeleton.

Lila

Drubin

1997

MBoC

164

219

View full text Add to dashboard Cite

show abstract

“…It is becoming clear that the ADF/cofilin (AC) family of proteins, which catalyze actin-filament severing and depolymerization in cells (reviewed by Moon and Drubin, 1995;Sarmiere and Bamburg, 2003;Zigmond, 2004), is necessary for cell migration (reviewed by Bamburg and Wiggan, 2002). AC proteins are also known regulators of cell polarity, both in yeast (Drees et al, 2001;Okada et al, 2006) and also in migrating cell types, both to sustain already established polarity (Dawe et al, 2003) and to trigger cell polarization (Helen R. Dawe.…”

Section: Introductionmentioning

confidence: 99%

“…ACs are regulated in cells by several mechanisms (reviewed by Moon and Drubin, 1995;Sarmiere and Bamburg, 2003;Zigmond, 2004). In chick fibroblasts, AC is at least regulated by phosphorylation on serine 3 by LIM kinase (Dawe et al, 2003), which inactivates AC.…”

Section: Introductionmentioning

confidence: 99%

ADF/cofilin family proteins control formation of oriented actin-filament bundles in the cell body to trigger fibroblast polarization

Mseka

Bamburg

Cramer

2007

Journal of Cell Science

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How formation of the front and rear of a cell are coordinated during cell polarization in migrating cells is not well understood. Time-lapse microscopy of live primary chick embryo heart fibroblasts expressing GFP-actin show that, prior to cell polarization, polymerized actin in the cell body reorganizes to form oriented actin-filament bundles spanning the entire cell body. Within an average of 5 minutes of oriented actin bundles forming, localized cell-edge retraction initiates at either the side or at one end of the newly formed bundles and then elaborates around the nearest end of the bundles to form the cell rear, the first visual break in cell symmetry. Localized net protrusion occurs at the opposing end of the bundles to form the cell front and lags formation of the rear of the cell. Consequently, cells acquire full polarity and start to migrate in the direction of the long axis of the bundles, as previously documented for already migrating cells. When ADF/cofilin family protein activity or actin-filament disassembly is specifically blocked during cell polarization, reorganization of polymerized actin to form oriented actin-filament bundles in the cell body fails, and formation of the cell rear and front is inhibited. We conclude that formation of oriented actin-filament bundles in the cell body requires ADF/cofilin family proteins, and is an early event needed to coordinate the spatial location of the cell rear and front during fibroblast polarization.

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“…These reorganizations are coordinated by a plethora of actin binding proteins the functions of which may be controlled by numerous signals including Ca 2ϩ , phosphoinositides, pH, or reversible phosphorylation (1)(2)(3). Few actin binding proteins have been identified in higher plants, and little is known about the regulation of actin dynamics in plant cells.…”

mentioning

confidence: 99%

F-actin and G-actin binding are uncoupled by mutation of conserved tyrosine residues in maize actin depolymerizing factor (ZmADF)

Jiang

Weeds

Khan

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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Actin depolymerizing factors (ADF) are stimulus responsive actin cytoskeleton modulating proteins. They bind both monomeric actin (G-actin) and filamentous actin (F-actin) and, under certain conditions, F-actin binding is followed by filament severing. In this paper, using mutant maize ADF3 proteins, we demonstrate that the maize ADF3 binding of F-actin can be spatially distinguished from that of G-actin. One mutant, zmadf3-1, in which Tyr-103 and Ala-104 (equivalent to destrin Tyr-117 and Ala-118) have been replaced by phenylalanine and glycine, respectively, binds more weakly to both G-actin and F-actin compared with maize ADF3. A second mutant, zmadf3-2, in which both Tyr-67 and Tyr-70 are replaced by phenylalanine, shows an affinity for G-actin similar to maize ADF3, but F-actin binding is abolished. The two tyrosines, Tyr-67 and Tyr-70, are in the equivalent position to Tyr-82 and Tyr-85 of destrin, respectively. Using the tertiary structure of destrin, yeast cofilin, and Acanthamoeba actophorin, we discuss the implications of removing the aromatic hydroxyls of Tyr-82 and Tyr-85 (i.e., the effect of substituting phenylalanine for tyrosine) and conclude that Tyr-82 plays a critical role in stabilizing the tertiary structure that is essential for F-actin binding. We propose that this tertiary structure is maintained as a result of a hydrogen bond between the hydroxyl of Tyr-82 and the carbonyl of Tyr-117, which is located in the long ␣-helix; amino acid components of this helix (Leu-111 to Phe-128) have been implicated in G-actin and F-actin binding. The structures of human destrin and yeast cofilin indicate a hydrogen distance of 2.61 and 2.77 Å, respectively, with corresponding bond angles of 99.5°and 113°, close to the optimum for a strong hydrogen bond.

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The ADF/Cofilin Proteins: Stimulus-responsive Modulators of Actin Dynamics

Cited by 250 publications

References 84 publications

Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, an adenylyl cyclase-associated protein and the actin cytoskeleton.

Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, an adenylyl cyclase-associated protein and the actin cytoskeleton.

ADF/cofilin family proteins control formation of oriented actin-filament bundles in the cell body to trigger fibroblast polarization

F-actin and G-actin binding are uncoupled by mutation of conserved tyrosine residues in maize actin depolymerizing factor (ZmADF)

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