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PubMed1984

Evidence for an ATP cap at the ends of actin filaments and its regulation of the F-actin steady state.

The correlation between the time courses of actin polymerization under continuous sonication and the associated ATP hydrolysis has been studied. ATP hydrolysis was not mechanistically coupled to polymerization, i.e. not necessary for polymerization, but occurred on F-actin in a subsequent monomolecular reaction. Under sonication, polymerization was complete in 10 s while hydrolysis of ATP on the polymer required 200 s. A value of 0.023 s-1 was found for the first order rate constant of ATP hydrolysis on the polymer at 25 degrees C, pH 7.8, in the presence of 0.2 mM ATP, 0.1 mM CaCl2, and 1 mM MgCl2, independent of the F-actin concentration. The conversion of ATP X F-actin to ADP X F-actin was accompanied by an increase in fluorescence of a pyrenyl probe covalently attached to actin, consistent with a 2-fold greater fluorescence for ADP X F-actin than for ATP X F-actin, with a rate constant of 0.022 s-1. In contrast, the fluorescence of F-actin labeled with 7-chloro-4-nitrobenzeno-2-oxa-1,3-diazole did not change significantly when ATP or ADP was bound. The direct consequence of the uncoupling between polymerization and ATP hydrolysis is the formation of an ATP cap at the ends of the filaments, which maintains the stability of the polymer, while most of the filament contains bound ADP. The heterogeneity of the filament with respect to ATP and ADP results in a nonlinear relationship between the rate of elongation and the concentration of G-actin with a discontinuity at the critical concentration, where the rate of growth is zero. In this respect, F-actin in ATP behaves similarly to microtubules in GTP.

Actins↗
PubMed1983

Effect of Acanthamoeba profilin on the pre-steady state kinetics of actin polymerization and on the concentration of F-actin at steady state.

The interaction of Acanthamoeba actin and Acanthamoeba profilin was evaluated as a function of ionic conditions. In the presence of 2 mM MgCl2 or 1 mM MgCl2 and 50 mM KCl, profilin decreased the concentration of F-actin at steady state, and inhibited the rates of filament elongation and spontaneous nucleation and polymerization. All of the experimental data were quantitatively accounted for on the basis of a 1:1 complex between profilin and monomeric actin with a Kr between 4 and 9 microM, the same value obtained previously in the absence of MgCl2. Therefore, the Mg2+ concentration did not affect the KD of the profilin-actin complex in these experiments. On the other hand, profilin did greatly amplify the decrease in concentration of F-actin at steady state caused by lowering the Mg2+ concentration. This results from the effect of Mg2+ on the critical concentration of the actin monomer with which the profilin-actin complex is in equilibrium. When the Mg2+ concentration is lowered, the critical concentration of actin monomer increases so that more profilin-actin complex is formed. Thus, appreciably more F-actin depolymerizes than in the absence of profilin. In this way, profilin could function intracellularly to convert small changes in critical concentration into large changes in the concentration of F-actin.

Actins↗
PubMed1982

Cross-linking of actin filament networks by self-association and actin-binding macromolecules.

We have used low shear falling ball viscometry to measure the effects of actin purity, solution conditions, and cross-linking macromolecules on the formation of actin filament networks. Removal of minor contaminants from conventional muscle actin (Spudich, J. A., and Watt, S. (1971) J. Biol. Chem. 246, 4866-4871) by gel filtration (MacLean-Fletcher, S. and Pollard, T.D. (1980c) Biochem. Biophys. Res. Commun. 96, 18-27), greatly promotes the interaction of the filaments. Purified actin filaments form a gel (apparent viscosity greater than 12,000 cp) at approximately 2 mg/ml whereas approximately 12 mg/ml of conventional actin filaments have a viscosity of less than 400 cp. The apparent viscosity of the filaments depends on pH and the concentration of monovalent and divalent cations. The viscosity of purified action filaments is more sensitive to such variables when compared to that of conventional actin filaments. Together these experiments suggest that actin filament self-associations contribute to the stabilization of actin gels. A number of basic macromolecules, including aldolase, histones, lysozyme, polylysine, and RNase A can bind to and crosslink conventional actin filaments to form a gel. Since it is unlikely that all of these molecules are bound to actin in vivo, experimental approaches in addition to viscometry and sedimentation must be applied to prove that a given protein functions as an actin cross-linking protein in the cell.

Actins↗
PubMed1999

Disruption of the utrophin-actin interaction by monoclonal antibodies and prediction of an actin-binding surface of utrophin.

Monoclonal antibody (mAb) binding sites in the N-terminal actin-binding domain of utrophin have been identified using phage-displayed peptide libraries, and the mAbs have been used to probe functional regions of utrophin involved in actin binding. mAbs were characterized for their ability to interact with the utrophin actin-binding domain and to affect actin binding to utrophin in sedimentation assays. One of these antibodies was able to inhibit utrophin-F-actin binding and was shown to recognize a predicted helical region at residues 13-22 of utrophin, close to a previously predicted actin-binding site. Two other mAbs which did not affect actin binding recognized predicted loops in the second calponin homology domain of the utrophin actin-binding domain. Using the known three-dimensional structure of the homologous actin-binding domain of fimbrin, these results have enabled us to determine the likely orientation of the utrophin actin-binding domain with respect to the actin filament.

Actins↗
PubMed1997

The complex containing actin-related proteins Arp2 and Arp3 is required for the motility and integrity of yeast actin patches.

BACKGROUND: Structural modeling and biochemical experiments in vitro have implicated a multi-protein complex containing two actin-related proteins, Arp2 and Arp3, as a potential actin-filament nucleation factor. This 'Arp2/3 complex' has been identified in Acanthamoeba and human cells and has been shown to localize to regions involved in actin-based motility, such as the leading edge of moving cells and the 'tail' of actin that forms behind the intracellular pathogen Listeria. The function of this complex in vivo has not been characterized, however, and the sequences of the non-actin-related subunits remain to be determined. RESULTS: An Arp3 homologue from the budding yeast Saccharomyces cerevisiae was found to localize to cortical actin patches, highly motile structures that concentrate at sites of polarized growth during the yeast cell cycle. A conditional arp3 mutant allele inhibited cortical actin motility at the restrictive temperature and eventually disrupted actin patches. Most Arp3 protein is found in a multi-protein complex; we purified this complex and determined the sequences of each of the protein subunits using a high-accuracy mass peptide-mapping technique. The proteins found in the complex are similar to those in the Acanthamoeba and human Arp2/3 complexes except that the yeast complex lacks a 40 kDa subunit, which is therefore not required for the structural integrity of the complex. CONCLUSIONS: The Arp2/3 protein complex is conserved from yeast to man, and in yeast the complex is required in vivo for the motility and integrity of cortical actin patches. We hypothesize that these patches may move by a Listeria-like mechanism driven by actin polymerization.

Actin-Related Protein 2↗
PubMed2003

Haematopoietic lineage cell-specific protein 1 (HS1) promotes actin-related protein (Arp) 2/3 complex-mediated actin polymerization.

HS1 (haematopoietic lineage cell-specific gene protein 1), a prominent substrate of intracellular protein tyrosine kinases in haematopoietic cells, is implicated in the immune response to extracellular stimuli and in cell differentiation induced by cytokines. Although HS1 contains a 37-amino acid tandem repeat motif and a C-terminal Src homology 3 domain and is closely related to the cortical-actin-associated protein cortactin, it lacks the fourth repeat that has been shown to be essential for cortactin binding to filamentous actin (F-actin). In this study, we examined the possible role of HS1 in the regulation of the actin cytoskeleton. Immunofluorescent staining demonstrated that HS1 co-localizes in the cytoplasm of cells with actin-related protein (Arp) 2/3 complex, the primary component of the cellular machinery responsible for de novo actin assembly. Furthermore, recombinant HS1 binds directly to Arp2/3 complex with an equilibrium dissociation constant (K(d)) of 880 nM. Although HS1 is a modest F-actin-binding protein with a K(d) of 400 nM, it increases the rate of the actin assembly mediated by Arp2/3 complex, and promotes the formation of branched actin filaments induced by Arp2/3 complex and a constitutively activated peptide of N-WASP (neural Wiskott-Aldrich syndrome protein). Our data suggest that HS1, like cortactin, plays an important role in the modulation of actin assembly.

Actin-Related Protein 2↗
PubMed1996

Actin organization, bristle morphology, and viability are affected by actin capping protein mutations in Drosophila.

Regulation of actin filament length and orientation is important in many actin-based cellular processes. This regulation is postulated to occur through the action of actin-binding proteins. Many actin-binding proteins that modify actin in vitro have been identified, but in many cases, it is not known if this activity is physiologically relevant. Capping protein (CP) is an actin-binding protein that has been demonstrated to control filament length in vitro by binding to the barbed ends and preventing the addition or loss of actin monomers. To examine the in vivo role of CP, we have performed a molecular and genetic characterization of the beta subunit of capping protein from Drosophila melanogaster. We have identified mutations in the Drosophila beta subunit-these are the first CP mutations in a multicellular organism, and unlike CP mutations in yeast, they are lethal, causing death during the early larval stage. Adult files that are heterozygous for a pair of weak alleles have a defect in bristle morphology that is correlated to disorganized actin bundles in developing bristles. Our data demonstrate that CP has an essential function during development, and further suggest that CP is required to regulate actin assembly during the development of specialized structures that depend on actin for their morphology.

Actin Capping Proteins↗
PubMed1997

Xenopus actin depolymerizing factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails.

In contrast to the slow rate of depolymerization of pure actin in vitro, populations of actin filaments in vivo turn over rapidly. Therefore, the rate of actin depolymerization must be accelerated by one or more factors in the cell. Since the actin dynamics in Listeria monocytogenes tails bear many similarities to those in the lamellipodia of moving cells, we have used Listeria as a model system to isolate factors required for regulating the rapid actin filament turnover involved in cell migration. Using a cell-free Xenopus egg extract system to reproduce the Listeria movement seen in a cell, we depleted candidate depolymerizing proteins and analyzed the effect that their removal had on the morphology of Listeria tails. Immunodepletion of Xenopus actin depolymerizing factor (ADF)/cofilin (XAC) from Xenopus egg extracts resulted in Listeria tails that were approximately five times longer than the tails from undepleted extracts. Depletion of XAC did not affect the tail assembly rate, suggesting that the increased tail length was caused by an inhibition of actin filament depolymerization. Immunodepletion of Xenopus gelsolin had no effect on either tail length or assembly rate. Addition of recombinant wild-type XAC or chick ADF protein to XAC-depleted extracts restored the tail length to that of control extracts, while addition of mutant ADF S3E that mimics the phosphorylated, inactive form of ADF did not reduce the tail length. Addition of excess wild-type XAC to Xenopus egg extracts reduced the length of Listeria tails to a limited extent. These observations show that XAC but not gelsolin is essential for depolymerizing actin filaments that rapidly turn over in Xenopus extracts. We also show that while the depolymerizing activities of XAC and Xenopus extract are effective at depolymerizing normal filaments containing ADP, they are unable to completely depolymerize actin filaments containing AMPPNP, a slowly hydrolyzible ATP analog. This observation suggests that the substrate for XAC is the ADP-bound subunit of actin and that the lifetime of a filament is controlled by its nucleotide content.

Actin Cytoskeleton↗
PubMed2002

Spatial regulation of actin dynamics: a tropomyosin-free, actin-rich compartment at the leading edge.

Rapid polymerization of a network of short, branched actin filaments takes place at the leading edge of migrating cells, a compartment enriched in activators of actin polymerization such as the Arp2/3 complex and cofilin. Actin filaments elsewhere in the cell are long and unbranched. Results reported here show that the presence or absence of tropomyosin in these different actin-containing regions helps establish functionally distinct actin-containing compartments in the cell. Tropomyosin, an inhibitor of the Arp2/3 complex and cofilin function, was localized in relation to actin filaments, the Arp2/3 complex, and free barbed ends of actin filaments in MTLn3 cells, which rapidly extend flat lamellipodia following EGF stimulation. All tropomyosin isoforms examined using indirect immunofluorescence were relatively absent from the dynamic leading edge compartment, but did colocalize with actin structures deeper in the lamellipodium and in stress fibers. An in vitro light microscopy assay revealed that tropomyosin protects actin filaments from cofilin severing. The results suggest that tropomyosin-free actin filaments under the membrane can participate in rapid, dynamic processes that depend on interactions between the activities of the Arp2/3 complex and ADF/cofilin that tropomyosin inhibits elsewhere in the cell.

Actin Cytoskeleton↗
PubMed2003

Actin filament disassembling activity of Caenorhabditis elegans actin-interacting protein 1 (UNC-78) is dependent on filament binding by a specific ADF/cofilin isoform.

Actin-interacting protein 1 (AIP1) is a conserved WD-repeat protein that enhances actin filament disassembly only in the presence of actin depolymerizing factor (ADF)/cofilin. In the nematode Caenorhabditis elegans, an AIP1 ortholog is encoded by the unc-78 gene that is required for organized assembly of muscle actin filaments. We produced bacterially expressed UNC-78 protein and found that it enhances actin filament disassembly preferentially in the presence of a specific ADF/cofilin isoform. Extensive and rapid filament disassembly by UNC-78 was observed in the presence of UNC-60B, a muscle-specific C. elegans ADF/cofilin isoform. UNC-78 also reduced the rate of spontaneous polymerization and enhanced subunit dissociation from filaments in the presence of UNC-60B. However, in the presence of UNC-60A, a non-muscle C. elegans ADF/cofilin isoform, UNC-78 only slightly enhanced filament disassembly. Interestingly, UNC-78 failed to enhance disassembly by mouse muscle-type cofilin. Using mutant forms of UNC-60B, we demonstrated that the F-actin-specific binding site of UNC-60B at the C terminus is required for filament disassembly by UNC-78. UNC-78 was expressed in body wall muscle and co-localized with actin where UNC-60B was also present. Surprisingly, UNC-78 was co-localized with actin in unc-60B null mutants, suggesting that the AIP1-actin interaction is not dependent on ADF/cofilin in muscle. These results suggest that UNC-78 closely collaborates with UNC-60B to regulate actin dynamics in muscle cells.

Actin Cytoskeleton↗
PubMed2006

Actin turnover-dependent fast dissociation of capping protein in the dendritic nucleation actin network: evidence of frequent filament severing.

Actin forms the dendritic nucleation network and undergoes rapid polymerization-depolymerization cycles in lamellipodia. To elucidate the mechanism of actin disassembly, we characterized molecular kinetics of the major filament end-binding proteins Arp2/3 complex and capping protein (CP) using single-molecule speckle microscopy. We have determined the dissociation rates of Arp2/3 and CP as 0.048 and 0.58 s(-1), respectively, in lamellipodia of live XTC fibroblasts. This CP dissociation rate is three orders of magnitude faster than in vitro. CP dissociates slower from actin stress fibers than from the lamellipodial actin network, suggesting that CP dissociation correlates with actin filament dynamics. We found that jasplakinolide, an actin depolymerization inhibitor, rapidly blocked the fast CP dissociation in cells. Consistently, the coexpression of LIM kinase prolonged CP speckle lifetime in lamellipodia. These results suggest that cofilin-mediated actin disassembly triggers CP dissociation from actin filaments. We predict that filament severing and end-to-end annealing might take place fairly frequently in the dendritic nucleation actin arrays.

Actin Capping Proteins↗
PubMed2006

Understanding the role of the G-actin-binding domain of Ena/VASP in actin assembly.

The Ena/VASP and WASP family of proteins play distinct roles in actin cytoskeleton remodeling. Ena/VASP is linked to actin filament elongation, whereas WASP plays a role in filament nucleation and branching mediated by Arp2/3 complex. The molecular mechanisms controlling both processes are only emerging. Both Ena/VASP and WASP are multidomain proteins. They both present poly-Pro regions, which mediate the binding of profilin-actin, followed by G-actin-binding (GAB) domains of the WASP-homology 2 (WH2) type. However, the WH2 of Ena/VASP is somewhat different from that of WASP, and has been poorly characterized. Here we demonstrate that this WH2 binds profilin-actin with higher affinity than actin alone. The results are consistent with a model whereby allosteric modulation of affinity drives the transition of profilin-actin from the poly-Pro region to the WH2 and then to the barbed end of the filament during elongation. Therefore, the function of the WH2 in Ena/VASP appears to be to "process" profilin-actin for its incorporation at the barbed end of the growing filament. Conformational changes in the newly incorporated actin subunit, resulting either from nucleotide hydrolysis or from the G- to F-actin transition, may serve as a "sensor" for the processive stepping of Ena/VASP. Conserved domain architecture suggests that WASP may work similarly.

Actin Cytoskeleton↗
PubMed2002

A new internal mode in F-actin helps explain the remarkable evolutionary conservation of actin's sequence and structure.

Actin is one of the most highly conserved eukaryotic proteins. There are no amino acid changes between the chicken and human skeletal muscle isoforms, and the most dissimilar actins still share more than 85% sequence identity [1]. We suggest that large discrete internal modes of freedom within the actin filament may account for a significant component of this conservation, since each subunit must make multiple specific interactions with neighboring subunits. In support of this, we find that the same state of tilt of the actin subunit exists in both yeast and vertebrate striated muscle actin, and that in both the two domains undergo a "propeller rotation." A similar movement of domains has also been seen in hexokinase, Hsc70, and Arp2/3, all structural homologs of actin, suggesting that such an interdomain hinge motion is common to proteins in this superfamily. Subunit-subunit interactions within the actin filament involve sequence insertions that are not present in MreB, a bacterial homolog of actin. Remarkably, we find that in the tilted state actin subunits make new contacts with neighboring subunits that also involve these inserts, suggesting a key role for these elements in F-actin polymorphism.

Actin Depolymerizing Factors↗
PubMed1982

Purification and characterization of a new mammalian serum protein with the ability to inhibit actin polymerization and promote depolymerization of actin filaments.

A protein with capacity to bind G-actin and the ability to inhibit polymerization and promote depolymerization of actin filaments has been isolated from the serum of rabbit. The protein, SAIP (for serum actin inhibitory protein), has been purified by affinity chromatography of serum over actin-Sepharose followed by protein fractionation with ammonium sulfate and chromatography over DEAE-cellulose. Five milligrams of purified SAIP is obtained from 100 mL of serum. Rabbit SAIP is resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresis into two closely related polypeptides of 60000 and 56000 daltons, respectively (ratio 5.1:1). Each of these polypeptides consists of two isoelectric variants. SAIP binds to monomeric actin with a stoichiometry of 1:1 and a Kd of 0.12 microM. The SAIP-actin complex binds to DNase I. Actin polymerization is completely inhibited by incubation of actin with an equal concentration of SAIP. At equimolar concentrations to F-actin, SAIP induces complete depolymerization of the actin filaments. SAIP is also present in calf serum.

Actin Depolymerizing Factors↗
PubMed1983

Plasma actin depolymerizing factor has both calcium-dependent and calcium-independent effects on actin.

The effects of pig plasma actin depolymerizing factor (ADF) on both G-actin polymerization and F-actin fragmentation have been examined by using rabbit skeletal muscle actin labeled with N-(1-pyrenyl)iodoacetamide, a sensitive fluorescent probe for monomer to filament interconversion. Fluorescence data have been compared with results obtained by viscometry and by difference absorption measurements at 232 nm. Plasma ADF nucleates actin filament assembly in a Ca2+-dependent manner; actin polymerization rates are enhanced at greater than 10(-6) M Ca2+. The calcium concentration dependence of this effect, showing a shift in ADF nucleating capacity between 10(-6) and 10(-7) M Ca2+, is that expected for an intracellular regulatory effect, but in plasma, the protein would always be saturated with Ca2+. Although the rate of polymerization is markedly enhanced in the presence of calcium ions, the extent of polymerization (as determined by the amplitude of the fluorescence change or the specific viscosity) is reduced in the presence of ADF and shows little or no Ca2+ dependence. The critical concentration of actin monomers is increased in the presence of ADF whether calcium is present or not. When ADF is added to F-actin, there is an immediate fall in fluorescence. This conversion of filaments to monomers by ADF (as defined by the fluorescence changes) is unaffected by calcium concentration. Electron micrographs of F-actin treated with ADF show that the filaments are indeed shortened at both high and low calcium concentrations. Taken together, these observations are interpreted in terms of a model in which ADF has both Ca2+-sensitive and Ca2+-insensitive binding sites for actin.

Actin Depolymerizing Factors↗
PubMed1985

An actin-depolymerizing protein (destrin) from porcine kidney. Its action on F-actin containing or lacking tropomyosin.

An Mr 19 000 protein (destrin) that has the ability to rapidly depolymerize F-actin in a stoichiometric manner was purified from porcine kidney by sequential chromatography on DNase I-agarose, hydroxyapatite, and Sephadex G-75. Its actin-depolymerizing activity is reversibly controlled by changes in KCl concentration but is insensitive to Ca2+ concentration. The rate of depolymerization of F-actin by destrin is much faster than that of spontaneous depolymerization induced by dilution and is not markedly decreased by the addition of end-blocking reagents such as cytochalasin B. These results suggest that destrin depolymerizes F-actin by interacting directly with F-actin protomers. Binding of muscle tropomyosin to F-actin slows down the rate of destrin-induced depolymerization of F-actin by about 30-fold. The data suggest that the destrin-induced depolymerization occurs from the ends of F-actin when F-actin is complexed with tropomyosin, but it takes place from the entire length of F-actin in the absence of tropomyosin.

Actin Depolymerizing Factors↗
PubMed2006

Myosin heavy-chain kinase A from Dictyostelium possesses a novel actin-binding domain that cross-links actin filaments.

Myosin heavy-chain kinase A (MHCK A) catalyses the disassembly of myosin II filaments in Dictyostelium cells via myosin II heavy-chain phosphorylation. MHCK A possesses a 'coiled-coil'-enriched domain that mediates the oligomerization, cellular localization and actin-binding activities of the kinase. F-actin (filamentous actin) binding by the coiled-coil domain leads to a 40-fold increase in MHCK A activity. In the present study we examined the actin-binding characteristics of the coiled-coil domain as a means of identifying mechanisms by which MHCK A-mediated disassembly of myosin II filaments can be regulated in the cell. Co-sedimentation assays revealed that the coiled-coil domain of MHCK A binds co-operatively to F-actin with an apparent K(D) of approx. 0.5 muM and a stoichiometry of approx. 5:1 [actin/C(1-498)]. Further analyses indicate that the coiled-coil domain binds along the length of the actin filament and possesses at least two actin-binding regions. Quite surprisingly, we found that the coiled-coil domain cross-links actin filaments into bundles, indicating that MHCK A can affect the cytoskeleton in two important ways: (1) by driving myosin II-filament disassembly via myosin II heavy-chain phosphorylation, and (2) by cross-linking/bundling actin filaments. This discovery, along with other supporting data, suggests a model in which MHCK A-mediated bundling of actin filaments plays a central role in the recruitment and activation of the kinase at specific sites in the cell. Ultimately this provides a means for achieving the robust and highly localized disruption of myosin II filaments that facilitates polarized changes in cell shape during processes such as chemotaxis, cytokinesis and multicellular development.

Actin Cytoskeleton↗
PubMed2006

The actin-depolymerizing factor homology and charged/helical domains of drebrin and mAbp1 direct membrane binding and localization via distinct interactions with actin.

Cytoskeletal dynamics are important for efficient function of the secretory pathway. ADP-ribosylation factor, ARF1, triggers vesicle coat assembly and, in concert with Cdc42, regulates actin polymerization and molecular motor-based motility. Drebrin and mammalian Abp1 (mAbp1) are actin-binding proteins found previously to bind to Golgi membranes in an ARF1-dependent manner in vitro. Despite sharing homology through two shared actin binding domains, drebrin and mAbp1 have different subcellular localization and bind to distinct actin structures on the Golgi apparatus. We find that the actin-depolymerizing factor homology (ADFH) and charged/helical actin binding domains of drebrin and mAbp1 are sufficient for regulated binding to Golgi membranes and subcellular localization. We have used mutant proteins and chimeras between mAbp1 and drebrin to identify motifs that direct targeting. We find that a linker region between the ADFH and charged/helical domains confers Golgi binding properties to mAbp1. mAbp1 binds to a specific actin pool through its ADFH/linker domain that is not bound by drebrin. Drebrin localization to the cell surface was found to involve motifs within the charged/helical domain. Our results indicate that targeting of these proteins is directed through multiple distinct interactions with the actin cytoskeleton. The mechanisms for selective recruitment of mAbp1 and drebrin to Golgi membranes indicate how actin-based structures are able to select specific actin-binding proteins and, thus, carry out multiple different functions within cells.

Actin Depolymerizing Factors↗