13 results on '"Giorgio, Scita"'
Search Results
2. Chronic Replication Problems Impact Cell Morphology and Adhesion of DNA Ligase I Defective Cells.
- Author
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Paolo Cremaschi, Matteo Oliverio, Valentina Leva, Silvia Bione, Roberta Carriero, Giulia Mazzucco, Andrea Palamidessi, Giorgio Scita, Giuseppe Biamonti, and Alessandra Montecucco
- Subjects
Medicine ,Science - Abstract
Moderate DNA damage resulting from metabolic activities or sub-lethal doses of exogenous insults may eventually lead to cancer onset. Human 46BR.1G1 cells bear a mutation in replicative DNA ligase I (LigI) which results in low levels of replication-dependent DNA damage. This replication stress elicits a constitutive phosphorylation of the ataxia telangiectasia mutated (ATM) checkpoint kinase that fails to arrest cell cycle progression or to activate apoptosis or cell senescence. Stable transfection of wild type LigI, as in 7A3 cells, prevents DNA damage and ATM activation. Here we show that parental 46BR.1G1 and 7A3 cells differ in important features such as cell morphology, adhesion and migration. Comparison of gene expression profiles in the two cell lines detects Bio-Functional categories consistent with the morphological and migration properties of LigI deficient cells. Interestingly, ATM inhibition makes 46BR.1G1 more similar to 7A3 cells for what concerns morphology, adhesion and expression of cell-cell adhesion receptors. These observations extend the influence of the DNA damage response checkpoint pathways and unveil a role for ATM kinase activity in modulating cell biology parameters relevant to cancer progression.
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- 2015
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3. The Eps8/IRSp53/VASP network differentially controls actin capping and bundling in filopodia formation.
- Author
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Federico Vaggi, Andrea Disanza, Francesca Milanesi, Pier Paolo Di Fiore, Elisabetta Menna, Michela Matteoli, Nir S Gov, Giorgio Scita, and Andrea Ciliberto
- Subjects
Biology (General) ,QH301-705.5 - Abstract
There is a body of literature that describes the geometry and the physics of filopodia using either stochastic models or partial differential equations and elasticity and coarse-grained theory. Comparatively, there is a paucity of models focusing on the regulation of the network of proteins that control the formation of different actin structures. Using a combination of in-vivo and in-vitro experiments together with a system of ordinary differential equations, we focused on a small number of well-characterized, interacting molecules involved in actin-dependent filopodia formation: the actin remodeler Eps8, whose capping and bundling activities are a function of its ligands, Abi-1 and IRSp53, respectively; VASP and Capping Protein (CP), which exert antagonistic functions in controlling filament elongation. The model emphasizes the essential role of complexes that contain the membrane deforming protein IRSp53, in the process of filopodia initiation. This model accurately accounted for all observations, including a seemingly paradoxical result whereby genetic removal of Eps8 reduced filopodia in HeLa, but increased them in hippocampal neurons, and generated quantitative predictions, which were experimentally verified. The model further permitted us to explain how filopodia are generated in different cellular contexts, depending on the dynamic interaction established by Eps8, IRSp53 and VASP with actin filaments, thus revealing an unexpected plasticity of the signaling network that governs the multifunctional activities of its components in the formation of filopodia.
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- 2011
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- View/download PDF
4. Propagating cell-membrane waves driven by curved activators of actin polymerization.
- Author
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Barak Peleg, Andrea Disanza, Giorgio Scita, and Nir Gov
- Subjects
Medicine ,Science - Abstract
Cells exhibit propagating membrane waves which involve the actin cytoskeleton. One type of such membranal waves are Circular Dorsal Ruffles (CDR) which are related to endocytosis and receptor internalization. Experimentally, CDRs have been associated with membrane bound activators of actin polymerization of concave shape. We present experimental evidence for the localization of convex membrane proteins in these structures, and their insensitivity to inhibition of myosin II contractility in immortalized mouse embryo fibroblasts cell cultures. These observations lead us to propose a theoretical model which explains the formation of these waves due to the interplay between complexes that contain activators of actin polymerization and membrane-bound curved proteins of both types of curvature (concave and convex). Our model predicts that the activity of both types of curved proteins is essential for sustaining propagating waves, which are abolished when one type of curved activator is removed. Within this model waves are initiated when the level of actin polymerization induced by the curved activators is higher than some threshold value, which allows the cell to control CDR formation. We demonstrate that the model can explain many features of CDRs, and give several testable predictions. This work demonstrates the importance of curved membrane proteins in organizing the actin cytoskeleton and cell shape.
- Published
- 2011
- Full Text
- View/download PDF
5. Molecular basis for the dual function of Eps8 on actin dynamics: bundling and capping.
- Author
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Maud Hertzog, Francesca Milanesi, Larnele Hazelwood, Andrea Disanza, HongJun Liu, Emilie Perlade, Maria Grazia Malabarba, Sebastiano Pasqualato, Alessio Maiolica, Stefano Confalonieri, Christophe Le Clainche, Nina Offenhauser, Jennifer Block, Klemens Rottner, Pier Paolo Di Fiore, Marie-France Carlier, Niels Volkmann, Dorit Hanein, and Giorgio Scita
- Subjects
Biology (General) ,QH301-705.5 - Abstract
Actin capping and cross-linking proteins regulate the dynamics and architectures of different cellular protrusions. Eps8 is the founding member of a unique family of capping proteins capable of side-binding and bundling actin filaments. However, the structural basis through which Eps8 exerts these functions remains elusive. Here, we combined biochemical, molecular, and genetic approaches with electron microscopy and image analysis to dissect the molecular mechanism responsible for the distinct activities of Eps8. We propose that bundling activity of Eps8 is mainly mediated by a compact four helix bundle, which is contacting three actin subunits along the filament. The capping activity is mainly mediated by a amphipathic helix that binds within the hydrophobic pocket at the barbed ends of actin blocking further addition of actin monomers. Single-point mutagenesis validated these modes of binding, permitting us to dissect Eps8 capping from bundling activity in vitro. We further showed that the capping and bundling activities of Eps8 can be fully dissected in vivo, demonstrating the physiological relevance of the identified Eps8 structural/functional modules. Eps8 controls actin-based motility through its capping activity, while, as a bundler, is essential for proper intestinal morphogenesis of developing Caenorhabditis elegans.
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- 2010
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6. Loss of the actin remodeler Eps8 causes intestinal defects and improved metabolic status in mice.
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Arianna Tocchetti, Charlotte Blanche Ekalle Soppo, Fabio Zani, Fabrizio Bianchi, Maria Cristina Gagliani, Benedetta Pozzi, Jan Rozman, Ralf Elvert, Nicole Ehrhardt, Birgit Rathkolb, Corinna Moerth, Marion Horsch, Helmut Fuchs, Valérie Gailus-Durner, Johannes Beckers, Martin Klingenspor, Eckhard Wolf, Martin Hrabé de Angelis, Eugenio Scanziani, Carlo Tacchetti, Giorgio Scita, Pier Paolo Di Fiore, and Nina Offenhäuser
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Medicine ,Science - Abstract
BACKGROUND: In a variety of organisms, including mammals, caloric restriction improves metabolic status and lowers the incidence of chronic-degenerative diseases, ultimately leading to increased lifespan. METHODOLOGY/PRINCIPAL FINDINGS: Here we show that knockout mice for Eps8, a regulator of actin dynamics, display reduced body weight, partial resistance to age- or diet-induced obesity, and overall improved metabolic status. Alteration in the liver gene expression profile, in behavior and metabolism point to a calorie restriction-like phenotype in Eps8 knockout mice. Additionally, and consistent with a calorie restricted metabolism, Eps8 knockout mice show increased lifespan. The metabolic alterations in Eps8 knockout mice correlated with a significant reduction in intestinal fat absorption presumably caused by a 25% reduction in intestinal microvilli length. CONCLUSIONS/SIGNIFICANCE: Our findings implicate actin dynamics as a novel variable in the determination of longevity. Additionally, our observations suggest that subtle differences in energy balance can, over time, significantly affect bodyweight and metabolic status in mice.
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- 2010
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7. Requirements for F-BAR proteins TOCA-1 and TOCA-2 in actin dynamics and membrane trafficking during Caenorhabditis elegans oocyte growth and embryonic epidermal morphogenesis.
- Author
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Chiara Giuliani, Flavia Troglio, Zhiyong Bai, Falshruti B Patel, Adriana Zucconi, Maria Grazia Malabarba, Andrea Disanza, Theresia B Stradal, Giuseppe Cassata, Stefano Confalonieri, Jeffrey D Hardin, Martha C Soto, Barth D Grant, and Giorgio Scita
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Genetics ,QH426-470 - Abstract
The TOCA family of F-BAR-containing proteins bind to and remodel lipid bilayers via their conserved F-BAR domains, and regulate actin dynamics via their N-Wasp binding SH3 domains. Thus, these proteins are predicted to play a pivotal role in coordinating membrane traffic with actin dynamics during cell migration and tissue morphogenesis. By combining genetic analysis in Caenorhabditis elegans with cellular biochemical experiments in mammalian cells, we showed that: i) loss of CeTOCA proteins reduced the efficiency of Clathrin-mediated endocytosis (CME) in oocytes. Genetic interference with CeTOCAs interacting proteins WSP-1 and WVE-1, and other components of the WVE-1 complex, produced a similar effect. Oocyte endocytosis defects correlated well with reduced egg production in these mutants. ii) CeTOCA proteins localize to cell-cell junctions and are required for proper embryonic morphogenesis, to position hypodermal cells and to organize junctional actin and the junction-associated protein AJM-1. iii) Double mutant analysis indicated that the toca genes act in the same pathway as the nematode homologue of N-WASP/WASP, wsp-1. Furthermore, mammalian TOCA-1 and C. elegans CeTOCAs physically associated with N-WASP and WSP-1 directly, or WAVE2 indirectly via ABI-1. Thus, we propose that TOCA proteins control tissues morphogenesis by coordinating Clathrin-dependent membrane trafficking with WAVE and N-WASP-dependent actin-dynamics.
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- 2009
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8. Eps8 regulates axonal filopodia in hippocampal neurons in response to brain-derived neurotrophic factor (BDNF).
- Author
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Elisabetta Menna, Andrea Disanza, Cinzia Cagnoli, Ursula Schenk, Giuliana Gelsomino, Emanuela Frittoli, Maud Hertzog, Nina Offenhauser, Corinna Sawallisch, Hans-Jürgen Kreienkamp, Frank B Gertler, Pier Paolo Di Fiore, Giorgio Scita, and Michela Matteoli
- Subjects
Biology (General) ,QH301-705.5 - Abstract
The regulation of filopodia plays a crucial role during neuronal development and synaptogenesis. Axonal filopodia, which are known to originate presynaptic specializations, are regulated in response to neurotrophic factors. The structural components of filopodia are actin filaments, whose dynamics and organization are controlled by ensembles of actin-binding proteins. How neurotrophic factors regulate these latter proteins remains, however, poorly defined. Here, using a combination of mouse genetic, biochemical, and cell biological assays, we show that genetic removal of Eps8, an actin-binding and regulatory protein enriched in the growth cones and developing processes of neurons, significantly augments the number and density of vasodilator-stimulated phosphoprotein (VASP)-dependent axonal filopodia. The reintroduction of Eps8 wild type (WT), but not an Eps8 capping-defective mutant, into primary hippocampal neurons restored axonal filopodia to WT levels. We further show that the actin barbed-end capping activity of Eps8 is inhibited by brain-derived neurotrophic factor (BDNF) treatment through MAPK-dependent phosphorylation of Eps8 residues S624 and T628. Additionally, an Eps8 mutant, impaired in the MAPK target sites (S624A/T628A), displays increased association to actin-rich structures, is resistant to BDNF-mediated release from microfilaments, and inhibits BDNF-induced filopodia. The opposite is observed for a phosphomimetic Eps8 (S624E/T628E) mutant. Thus, collectively, our data identify Eps8 as a critical capping protein in the regulation of axonal filopodia and delineate a molecular pathway by which BDNF, through MAPK-dependent phosphorylation of Eps8, stimulates axonal filopodia formation, a process with crucial impacts on neuronal development and synapse formation.
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- 2009
- Full Text
- View/download PDF
9. Coordination of membrane and actin cytoskeleton dynamics during filopodia protrusion.
- Author
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Changsong Yang, Matthew Hoelzle, Andrea Disanza, Giorgio Scita, and Tatyana Svitkina
- Subjects
Medicine ,Science - Abstract
Leading edge protrusion of migrating cells involves tightly coordinated changes in the plasma membrane and actin cytoskeleton. It remains unclear whether polymerizing actin filaments push and deform the membrane, or membrane deformation occurs independently and is subsequently stabilized by actin filaments. To address this question, we employed an ability of the membrane-binding I-BAR domain of IRSp53 to uncouple the membrane and actin dynamics and to induce filopodia in expressing cells. Using time-lapse imaging and electron microscopy of IRSp53-I-BAR-expressing B16F1 melanoma cells, we demonstrate that cells are not able to protrude or maintain durable long extensions without actin filaments in their interior, but I-BAR-dependent membrane deformation can create a small and transient space at filopodial tips that is subsequently filled with actin filaments. Moreover, the expressed I-BAR domain forms a submembranous coat that may structurally support these transient actin-free protrusions until they are further stabilized by the actin cytoskeleton. Actin filaments in the I-BAR-induced filopodia, in contrast to normal filopodia, do not have a uniform length, are less abundant, poorly bundled, and display erratic dynamics. Such unconventional structural organization and dynamics of actin in I-BAR-induced filopodia suggests that a typical bundle of parallel actin filaments is not necessary for generation and mechanical support of the highly asymmetric filopodial geometry. Together, our data suggest that actin filaments may not directly drive the protrusion, but only stabilize the space generated by the membrane deformation; yet, such stabilization is necessary for efficient protrusion.
- Published
- 2009
- Full Text
- View/download PDF
10. Novel roles of formin mDia2 in lamellipodia and filopodia formation in motile cells.
- Author
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Changsong Yang, Lubov Czech, Silke Gerboth, Shin-ichiro Kojima, Giorgio Scita, and Tatyana Svitkina
- Subjects
Biology (General) ,QH301-705.5 - Abstract
Actin polymerization-driven protrusion of the leading edge is a key element of cell motility. The important actin nucleators formins and the Arp2/3 complex are believed to have nonoverlapping functions in inducing actin filament bundles in filopodia and dendritic networks in lamellipodia, respectively. We tested this idea by investigating the role of mDia2 formin in leading-edge protrusion by loss-of-function and gain-of-function approaches. Unexpectedly, mDia2 depletion by short interfering RNA (siRNA) severely inhibited lamellipodia. Structural analysis of the actin network in the few remaining lamellipodia suggested an mDia2 role in generation of long filaments. Consistently, constitutively active mDia2 (DeltaGBD-mDia2) induced accumulation of long actin filaments in lamellipodia and increased persistence of lamellipodial protrusion. Depletion of mDia2 also inhibited filopodia, whereas expression of DeltaGBD-mDia2 promoted their formation. Correlative light and electron microscopy showed that DeltaGBD-mDia2-induced filopodia were formed from lamellipodial network through gradual convergence of long lamellipodial filaments into bundles. Efficient filopodia induction required mDia2 targeting to the membrane, likely through a scaffolding protein Abi1. Furthermore, mDia2 and Abi1 interacted through the N-terminal regulatory sequences of mDia2 and the SH3-containing Abi1 sequences. We propose that mDia2 plays an important role in formation of lamellipodia by nucleating and/or protecting from capping lamellipodial actin filaments, which subsequently exhibit high tendency to converge into filopodia.
- Published
- 2007
- Full Text
- View/download PDF
11. Eps8 Regulates Axonal Filopodia in Hippocampal Neurons in Response to Brain-Derived Neurotrophic Factor (BDNF)
- Author
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Elisabetta Menna, Andrea Disanza, Cinzia Cagnoli, Ursula Schenk, Giuliana Gelsomino, Emanuela Frittoli, Maud Hertzog, Nina Offenhauser, Corinna Sawallisch, Hans-Jürgen Kreienkamp, Frank B. Gertler, Pier Paolo Di Fiore, Giorgio Scita, and Michela Matteoli
- Subjects
Male ,QH301-705.5 ,Green Fluorescent Proteins ,Hippocampal formation ,Biology ,Transfection ,Hippocampus ,General Biochemistry, Genetics and Molecular Biology ,Cell Line ,EPS8 ,Mice ,Animals ,Humans ,Pseudopodia ,Phosphorylation ,Biology (General) ,Cells, Cultured ,Adaptor Proteins, Signal Transducing ,Brain-derived neurotrophic factor ,Mice, Knockout ,Neurons ,General Immunology and Microbiology ,General Neuroscience ,Brain-Derived Neurotrophic Factor ,Correction ,Anatomy ,Actins ,Axons ,Rats ,Mice, Inbred C57BL ,Cytoskeletal Proteins ,Microscopy, Fluorescence ,Female ,RNA Interference ,Mitogen-Activated Protein Kinases ,General Agricultural and Biological Sciences ,Neuroscience ,Filopodia - Abstract
The regulation of filopodia plays a crucial role during neuronal development and synaptogenesis. Axonal filopodia, which are known to originate presynaptic specializations, are regulated in response to neurotrophic factors. The structural components of filopodia are actin filaments, whose dynamics and organization are controlled by ensembles of actin-binding proteins. How neurotrophic factors regulate these latter proteins remains, however, poorly defined. Here, using a combination of mouse genetic, biochemical, and cell biological assays, we show that genetic removal of Eps8, an actin-binding and regulatory protein enriched in the growth cones and developing processes of neurons, significantly augments the number and density of vasodilator-stimulated phosphoprotein (VASP)-dependent axonal filopodia. The reintroduction of Eps8 wild type (WT), but not an Eps8 capping-defective mutant, into primary hippocampal neurons restored axonal filopodia to WT levels. We further show that the actin barbed-end capping activity of Eps8 is inhibited by brain-derived neurotrophic factor (BDNF) treatment through MAPK-dependent phosphorylation of Eps8 residues S624 and T628. Additionally, an Eps8 mutant, impaired in the MAPK target sites (S624A/T628A), displays increased association to actin-rich structures, is resistant to BDNF-mediated release from microfilaments, and inhibits BDNF-induced filopodia. The opposite is observed for a phosphomimetic Eps8 (S624E/T628E) mutant. Thus, collectively, our data identify Eps8 as a critical capping protein in the regulation of axonal filopodia and delineate a molecular pathway by which BDNF, through MAPK-dependent phosphorylation of Eps8, stimulates axonal filopodia formation, a process with crucial impacts on neuronal development and synapse formation.
- Published
- 2015
12. Propagating Cell-Membrane Waves Driven by Curved Activators of Actin Polymerization
- Author
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Nir S. Gov, Giorgio Scita, Andrea Disanza, and Barak Peleg
- Subjects
Biophysics ,lcsh:Medicine ,Arp2/3 complex ,Actin Filaments ,macromolecular substances ,Biophysics Simulations ,Biophysics Theory ,Cell membrane ,Mice ,Biopolymers ,Molecular Cell Biology ,Myosin ,medicine ,Animals ,Cell Mechanics ,Biomechanics ,lcsh:Science ,Cytoskeleton ,Biology ,Actin ,Cell Line, Transformed ,Multidisciplinary ,biology ,Physics ,lcsh:R ,Cell Membrane ,Membrane Proteins ,Computational Biology ,Actin remodeling ,Actin cytoskeleton ,Actins ,Cellular Structures ,Cell biology ,Cell Motility ,medicine.anatomical_structure ,Microscopy, Fluorescence ,Membrane protein ,biology.protein ,lcsh:Q ,Biophysic Al Simulations ,Membranes and Sorting ,Research Article - Abstract
Cells exhibit propagating membrane waves which involve the actin cytoskeleton. One type of such membranal waves are Circular Dorsal Ruffles (CDR) which are related to endocytosis and receptor internalization. Experimentally, CDRs have been associated with membrane bound activators of actin polymerization of concave shape. We present experimental evidence for the localization of convex membrane proteins in these structures, and their insensitivity to inhibition of myosin II contractility in immortalized mouse embryo fibroblasts cell cultures. These observations lead us to propose a theoretical model which explains the formation of these waves due to the interplay between complexes that contain activators of actin polymerization and membrane-bound curved proteins of both types of curvature (concave and convex). Our model predicts that the activity of both types of curved proteins is essential for sustaining propagating waves, which are abolished when one type of curved activator is removed. Within this model waves are initiated when the level of actin polymerization induced by the curved activators is higher than some threshold value, which allows the cell to control CDR formation. We demonstrate that the model can explain many features of CDRs, and give several testable predictions. This work demonstrates the importance of curved membrane proteins in organizing the actin cytoskeleton and cell shape.
- Published
- 2011
13. Novel Roles of Formin mDia2 in Lamellipodia and Filopodia Formation in Motile Cells
- Author
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Shin-ichiro Kojima, Silke Gerboth, Lubov Czech, Giorgio Scita, Tatyana Svitkina, and Changsong Yang
- Subjects
animal structures ,QH301-705.5 ,Formins ,Gene Expression ,macromolecular substances ,Actin-Related Protein 2-3 Complex ,General Biochemistry, Genetics and Molecular Biology ,Mice ,03 medical and health sciences ,0302 clinical medicine ,Cell Movement ,Animals ,Humans ,Gene Silencing ,Pseudopodia ,Biology (General) ,RNA, Small Interfering ,Cytoskeleton ,Adaptor Proteins, Signal Transducing ,030304 developmental biology ,0303 health sciences ,General Immunology and Microbiology ,biology ,General Neuroscience ,Cell Membrane ,Cell Biology ,Cell biology ,Cytoskeletal Proteins ,Paracytophagy ,Microscopy, Electron, Scanning ,biology.protein ,MDia1 ,Lamellipodium ,Carrier Proteins ,General Agricultural and Biological Sciences ,Filopodia ,030217 neurology & neurosurgery ,Research Article ,HeLa Cells - Abstract
Actin polymerization-driven protrusion of the leading edge is a key element of cell motility. The important actin nucleators formins and the Arp2/3 complex are believed to have nonoverlapping functions in inducing actin filament bundles in filopodia and dendritic networks in lamellipodia, respectively. We tested this idea by investigating the role of mDia2 formin in leading-edge protrusion by loss-of-function and gain-of-function approaches. Unexpectedly, mDia2 depletion by short interfering RNA (siRNA) severely inhibited lamellipodia. Structural analysis of the actin network in the few remaining lamellipodia suggested an mDia2 role in generation of long filaments. Consistently, constitutively active mDia2 (ΔGBD-mDia2) induced accumulation of long actin filaments in lamellipodia and increased persistence of lamellipodial protrusion. Depletion of mDia2 also inhibited filopodia, whereas expression of ΔGBD-mDia2 promoted their formation. Correlative light and electron microscopy showed that ΔGBD-mDia2–induced filopodia were formed from lamellipodial network through gradual convergence of long lamellipodial filaments into bundles. Efficient filopodia induction required mDia2 targeting to the membrane, likely through a scaffolding protein Abi1. Furthermore, mDia2 and Abi1 interacted through the N-terminal regulatory sequences of mDia2 and the SH3-containing Abi1 sequences. We propose that mDia2 plays an important role in formation of lamellipodia by nucleating and/or protecting from capping lamellipodial actin filaments, which subsequently exhibit high tendency to converge into filopodia., Author Summary Cell motility is a cyclic process, with the protrusion of the leading edge followed by retraction of the rear. Protrusion is driven by polymerization of actin filaments, with the spatial organization of these filaments determining the shape of the protrusions. For example, the spike-like filopodia contain bundles of long actin filaments, whereas the sheet-like lamellipodia contain branched actin networks. In biochemical assays, two stimulators of actin polymerization, Arp2/3 complex and formins, induce branched or individual filaments, respectively. In cells, Arp2/3 complex and formins also appear to be implicated in the formation of lamellipodia and filopodia, respectively. However, when we investigated the role of mDia2 formin by functional approaches, we unexpectedly found that it is essential, not only for filopodia, but also for lamellipodia. Moreover, functions of mDia2 in lamellipodia and filopodia appeared intimately linked. We recorded behavior of cells by light microscopy and then used electron microscopy to study actin architecture in the same cells. We found that an activated form of mDia2 was first recruited to lamellipodia, where it induced many long, unbranched filaments, and from there, drove formation of filopodia through gradual convergence of these lamellipodial filaments into bundles. These data demonstrate a strong relationship between structurally different actin filament arrays and molecular machineries involved in their formation., Formin mDia2 was believed to function mainly in the generation of filopodia in migrating cells. We unexpectedly found that mDia2 is also important for lamellipodia and induces filopodia in association with lamellipodia.
- Published
- 2007
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