FMNL2 drives actin-based protrusion and migration downstream of Cdc42. - Test2 - elhamkhani - TriplyDB

FMNL2 drives actin-based protrusion and migration downstream of Cdc42.

FMNL2 drives actin-based protrusion and migration downstream of Cdc42.

http://www.wikidata.org/entity/Q42188467

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Alterations of the apical junctional complex and actin cytoskeleton and their role in colorectal cancer progression Formins at a glance Cell type-dependent mechanisms for formin-mediated assembly of filopodia.α5β1 integrin recycling promotes Arp2/3-independent cancer cell invasion via the formin FHOD3.Junctional actin assembly is mediated by Formin-like 2 downstream of Rac1.Functional hierarchy of redundant actin assembly factors revealed by fine-grained registration of intrinsic image fluctuations.Formin and capping protein together embrace the actin filament in a ménage à trois.Ligand-induced activation of a formin-NPF pair leads to collaborative actin nucleation WAVE binds Ena/VASP for enhanced Arp2/3 complex-based actin assembly.The formins FMNL1 and mDia1 regulate coiling phagocytosis of Borrelia burgdorferi by primary human macrophages.Optical control of protein activity by fluorescent protein domains.The F-BAR protein Cip4/Toca-1 antagonizes the formin Diaphanous in membrane stabilization and compartmentalization.Arp2/3 complex is essential for actin network treadmilling as well as for targeting of capping protein and cofilin.The formin FHOD1 and the small GTPase Rac1 promote vaccinia virus actin-based motility.Ena/VASP Enabled is a highly processive actin polymerase tailored to self-assemble parallel-bundled F-actin networks with Fascin New single-molecule speckle microscopy reveals modification of the retrograde actin flow by focal adhesions at nanometer scales.The formin FMNL3 assembles plasma membrane protrusions that participate in cell-cell adhesion.FMNL formins boost lamellipodial force generation.Myristoylation: An Important Protein Modification in the Immune Response Characterization of Leukocyte Formin FMNL1 Expression in Human Tissues.VEZT, a novel putative tumor suppressor, suppresses the growth and tumorigenicity of gastric cancer.Novel roles for actin in mitochondrial fission Metastasis suppressor microRNA-335 targets the formin family of actin nucleators.Two functionally distinct sources of actin monomers supply the leading edge of lamellipodia A specific FMNL2 isoform is up-regulated in invasive cells Emergence of an Apical Epithelial Cell Surface In Vivo Comparative gene expression analysis of the fmnl family of formins during zebrafish development and implications for tissue specific functions.Unique and Overlapping Functions of Formins Frl and DAAM During Ommatidial Rotation and Neuronal Development in Drosophila FMNL2/FMNL3 formins are linked with oncogenic pathways and predict melanoma outcome.ARP2/3-dependent growth in the plant kingdom: SCARs for life.A Diaphanous-related formin links Ras signaling directly to actin assembly in macropinocytosis and phagocytosis.A role for myosin II in mammalian mitochondrial fission.New insights into the regulation and cellular functions of the ARP2/3 complex.RhoA, RhoB and RhoC have different roles in cancer cell migration.Small Rho GTPases in the control of cell shape and mobility.Actin dynamics, architecture, and mechanics in cell motility.Transcriptomic network support distinct roles of classical and non-classical monocytes in human.Bacterial subversion of host cytoskeletal machinery: hijacking formins and the Arp2/3 complex.Formins as effector proteins of Rho GTPases Self-organization of protrusions and polarity during eukaryotic chemotaxis.

P2860

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P2860

FMNL2 drives actin-based protrusion and migration downstream of Cdc42.

http://www.wikidata.org/entity/Q42188467

description

2012 nî lūn-bûn

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2012年の論文

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年學術文章

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2012年學術文章

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2012年學術文章

@zh-hant

name

FMNL2 drives actin-based protrusion and migration downstream of Cdc42.

@en

FMNL2 drives actin-based protrusion and migration downstream of Cdc42.

@nl

type

label

FMNL2 drives actin-based protrusion and migration downstream of Cdc42.

@en

FMNL2 drives actin-based protrusion and migration downstream of Cdc42.

@nl

prefLabel

FMNL2 drives actin-based protrusion and migration downstream of Cdc42.

@en

FMNL2 drives actin-based protrusion and migration downstream of Cdc42.

@nl

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J.CUB.2012.03.064

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Current Biology

P1476

FMNL2 drives actin-based protrusion and migration downstream of Cdc42

@en

P2093

Dennis Breitsprecher

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

Jan Faix

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

Jennifer Block

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Moritz Winterhoff

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

Patrick Duwe

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

Robert Geffers

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

Sonja Kühn

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P2860

Autoinhibition regulates cellular localization and actin assembly activity of the diaphanous-related formins FRLalpha and mDia1.

Novel roles of formin mDia2 in lamellipodia and filopodia formation in motile cells

Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia

Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells.

A nucleator arms race: cellular control of actin assembly

Cdc42 is not essential for filopodium formation, directed migration, cell polarization, and mitosis in fibroblastoid cells

Filopodia formation in the absence of functional WAVE- and Arp2/3-complexes.

Arp2/3 complex interactions and actin network turnover in lamellipodia.

Cdc42 and Rac family GTPases regulate mode and speed but not direction of primary fibroblast migration during platelet-derived growth factor-dependent chemotaxis

Arp2 depletion inhibits sheet-like protrusions but not linear protrusions of fibroblasts and lymphocytes

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1005-1012

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scholarly article

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10.1016/J.CUB.2012.03.064

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11

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22

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Cord Brakebusch

Klemens Rottner

Theresia Stradal

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2012-05-17T00:00:00Z

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225047951

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22608513

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3765947

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