Ena/VASP proteins capture actin filament barbed ends. - Wikidata - awgldk - TriplyDB

Ena/VASP proteins capture actin filament barbed ends.

Ena/VASP proteins capture actin filament barbed ends.

http://www.wikidata.org/entity/Q30439841

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Mena deficiency delays tumor progression and decreases metastasis in polyoma middle-T transgenic mouse mammary tumors CDC42 switches IRSp53 from inhibition of actin growth to elongation by clustering of VASP Ena/VASP: towards resolving a pointed controversy at the barbed end Clustering of VASP actively drives processive, WH2 domain-mediated actin filament elongation.Regulation of the Postsynaptic Compartment of Excitatory Synapses by the Actin Cytoskeleton in Health and Its Disruption in Disease Capping protein regulators fine-tune actin assembly dynamics 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.Eps8 regulates axonal filopodia in hippocampal neurons in response to brain-derived neurotrophic factor (BDNF)α-Actinin-4/FSGS1 is required for Arp2/3-dependent actin assembly at the adherens junction Modeling capping protein FRAP and CALI experiments reveals in vivo regulation of actin dynamics.Zyxin-mediated actin assembly is required for efficient wound closure.Molecular mechanism of Ena/VASP-mediated actin-filament elongation.Ena/VASP Enabled is a highly processive actin polymerase tailored to self-assemble parallel-bundled F-actin networks with Fascin The actin regulators Enabled and Diaphanous direct distinct protrusive behaviors in different tissues during Drosophila development.The Eps8/IRSp53/VASP network differentially controls actin capping and bundling in filopodia formation PKA-regulated VASP phosphorylation promotes extrusion of transformed cells from the epithelium Ena/VASP regulates mDia2-initiated filopodial length, dynamics, and function.Actin filament attachments for sustained motility in vitro are maintained by filament bundling.Ena/VASP proteins cooperate with the WAVE complex to regulate the actin cytoskeleton.Loss of profilin-1 expression enhances breast cancer cell motility by Ena/VASP proteins VASP is a processive actin polymerase that requires monomeric actin for barbed end association.The growth cone cytoskeleton in axon outgrowth and guidance.Mena invasive (MenaINV) promotes multicellular streaming motility and transendothelial migration in a mouse model of breast cancer Profilin1 regulates invadopodium maturation in human breast cancer cells Selectivity in subunit composition of Ena/VASP tetramers.Protein localization by actin treadmilling and molecular motors regulates stereocilia shape and treadmilling rate.A Mena invasion isoform potentiates EGF-induced carcinoma cell invasion and metastasis Actin nucleation and elongation factors: mechanisms and interplay.Ena/VASP: proteins at the tip of the nervous system.Differential VASP phosphorylation controls remodeling of the actin cytoskeleton.Actin filament nucleation and elongation factors--structure-function relationships.Regulation of actin cytoskeleton dynamics in cells.Actin machinery and mechanosensitivity in invadopodia, podosomes and focal adhesions.Structural insights into de novo actin polymerization.Metastasis: tumor cells becoming MENAcing.Control of actin filament dynamics at barbed ends by WH2 domains: from capping to permissive and processive assembly.Actin dynamics, architecture, and mechanics in cell motility.Steering cell migration: lamellipodium dynamics and the regulation of directional persistence.WAVE2, N-WASP, and Mena facilitate cell invasion via phosphatidylinositol 3-kinase-dependent local accumulation of actin filaments.

P2860

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P2860

Ena/VASP proteins capture actin filament barbed ends.

http://www.wikidata.org/entity/Q30439841

description

2008 nî lūn-bûn

@nan

2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի փետրվարին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

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name

Ena/VASP proteins capture actin filament barbed ends.

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Ena/VASP proteins capture actin filament barbed ends.

@en

type

label

Ena/VASP proteins capture actin filament barbed ends.

@ast

Ena/VASP proteins capture actin filament barbed ends.

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prefLabel

Ena/VASP proteins capture actin filament barbed ends.

@ast

Ena/VASP proteins capture actin filament barbed ends.

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Journal of Biological Chemistry

P1476

Ena/VASP proteins capture actin filament barbed ends.

@en

P2093

Dorothy A Schafer

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Lejla Pasic

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

Tatyana Kotova

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P2860

Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP.

Cortactin, an 80/85-kilodalton pp60src substrate, is a filamentous actin-binding protein enriched in the cell cortex

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

Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex.

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

Emergence of large-scale cell morphology and movement from local actin filament growth dynamics

The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation

Single molecule kinetic analysis of actin filament capping. Polyphosphoinositides do not dissociate capping proteins

Interactions with PIP2, ADP-actin monomers, and capping protein regulate the activity and localization of yeast twinfilin

The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin

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9814-9819

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scholarly article

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10.1074/JBC.M710475200

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15

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283

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18283104

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2442276

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