Ena/VASP proteins enhance actin polymerization in the presence of barbed end capping proteins - Wikidata - awgldk - TriplyDB

Ena/VASP proteins enhance actin polymerization in the presence of barbed end capping proteins

Ena/VASP proteins enhance actin polymerization in the presence of barbed end capping proteins

http://www.wikidata.org/entity/Q24678535

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Mena deficiency delays tumor progression and decreases metastasis in polyoma middle-T transgenic mouse mammary tumors Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP.Coronin 1B coordinates Arp2/3 complex and cofilin activities at the leading edge CDC42 switches IRSp53 from inhibition of actin growth to elongation by clustering of VASP Dynamic length regulation of sensory stereocilia Ena/VASP: towards resolving a pointed controversy at the barbed end Clustering of VASP actively drives processive, WH2 domain-mediated actin filament elongation.Capping protein regulators fine-tune actin assembly dynamics Cell type-dependent mechanisms for formin-mediated assembly of filopodia.Lamellipodin promotes invasive 3D cancer cell migration via regulated interactions with Ena/VASP and SCAR/WAVE.Reconstitution of actin-based motility by vasodilator-stimulated phosphoprotein (VASP) depends on the recruitment of F-actin seeds from the solution produced by cofilin.Profilin-1 serves as a gatekeeper for actin assembly by Arp2/3-dependent and -independent pathways.The Drosophila actin regulator ENABLED regulates cell shape and orientation during gonad morphogenesis Eps8 regulates axonal filopodia in hippocampal neurons in response to brain-derived neurotrophic factor (BDNF)Novel roles of formin mDia2 in lamellipodia and filopodia formation in motile cells Emergence of large-scale cell morphology and movement from local actin filament growth dynamics Human Mena associates with Rac1 small GTPase in glioblastoma cell lines The solution structure of pGolemi, a high affinity Mena EVH1 binding miniature protein, suggests explanations for paralog-specific binding to Ena/VASP homology (EVH) 1 domains The cytoskeleton and neurite initiation Arp2/3 complex is important for filopodia formation, growth cone motility, and neuritogenesis in neuronal cells Single molecule kinetic analysis of actin filament capping. Polyphosphoinositides do not dissociate capping proteins A crucial role in cell spreading for the interaction of Abl PxxP motifs with Crk and Nck adaptors.Short-term retention of actin filament binding proteins on lamellipodial actin bundles.WAVE binds Ena/VASP for enhanced Arp2/3 complex-based actin assembly.Vasodilator-stimulated phosphoprotein (VASP) induces actin assembly in dendritic spines to promote their development and potentiate synaptic strength.Ena/VASP proteins capture actin filament barbed ends.Ena/VASP proteins have an anti-capping independent function in filopodia formation.Ena/VASP proteins can regulate distinct modes of actin organization at cadherin-adhesive contacts.The bundling activity of vasodilator-stimulated phosphoprotein is required for filopodium formation.Diffusion rate limitations in actin-based propulsion of hard and deformable particles.VASP governs actin dynamics by modulating filament anchoring.Enhanced EGFP-chromophore-assisted laser inactivation using deficient cells rescued with functional EGFP-fusion proteins.Actin turnover-dependent fast dissociation of capping protein in the dendritic nucleation actin network: evidence of frequent filament severing.Using Bcr-Abl to examine mechanisms by which abl kinase regulates morphogenesis in Drosophila.Enabled and Capping protein play important roles in shaping cell behavior during Drosophila oogenesis The Arp2/3 complex, UNC-115/abLIM, and UNC-34/Enabled regulate axon guidance and growth cone filopodia formation in Caenorhabditis elegans.Exploring the roles of diaphanous and enabled activity in shaping the balance between filopodia and lamellipodia.Modeling capping protein FRAP and CALI experiments reveals in vivo regulation of actin dynamics.Ena drives invasive macrophage migration in Drosophila embryos.Molecular mechanism of Ena/VASP-mediated actin-filament elongation.

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P2860

Ena/VASP proteins enhance actin polymerization in the presence of barbed end capping proteins

http://www.wikidata.org/entity/Q24678535

description

2005 nî lūn-bûn

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2005 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2005年の論文

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Ena/VASP proteins enhance acti ...... of barbed end capping proteins

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Ena/VASP proteins enhance acti ...... of barbed end capping proteins

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Journal of Biological Chemistry

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Ena/VASP proteins enhance acti ...... of barbed end capping proteins

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P2093

Dorit Hanein

http://www.w3.org/2001/XMLSchema#string

Dorothy A Schafer

http://www.w3.org/2001/XMLSchema#string

Frank B Gertler

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Larnele Hazelwood

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Tatyana I Kotova

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P2860

A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family.

The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat

The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins

VASP protects actin filaments from gelsolin: an in vitro study with implications for platelet actin reorganizations

Pivotal role of VASP in Arp2/3 complex-mediated actin nucleation, actin branch-formation, and Listeria monocytogenes motility

Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes

Trisoxazole macrolide toxins mimic the binding of actin-capping proteins to actin

Structure of gelsolin segment 1-actin complex and the mechanism of filament severing

EMAN: semiautomated software for high-resolution single-particle reconstructions

Formin leaky cap allows elongation in the presence of tight capping proteins.

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28653-28662

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scholarly article

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2960026

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10.1074/JBC.M503957200

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31

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280

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15939738

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1747414

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