The mammalian verprolin homologue WIRE participates in receptor-mediated endocytosis and regulation of the actin filament system by distinct mechanisms (Q57362520)

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English	The mammalian verprolin homologue WIRE participates in receptor-mediated endocytosis and regulation of the actin filament system by distinct mechanisms	No description defined

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The mammalian verprolin homologue WIRE participates in receptor-mediated endocytosis and regulation of the actin filament system by distinct mechanisms (English)

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Pontus Aspenström

1

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publication date

August 2004

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Experimental Cell Research

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298

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2

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485-498

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T cell lines characterize events in the pathogenesis of the Wiskott-Aldrich syndrome

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N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases

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Genomic organization and expression profile of the human and mouse WAVE gene family

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WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac

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Identification of two human WAVE/SCAR homologues as general actin regulatory molecules which associate with the Arp2/3 complex

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The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly

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Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex

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A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases

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Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization

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Rho GTPases have diverse effects on the organization of the actin filament system

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WIP, a protein associated with Wiskott–Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells

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A homochiral metal-organic porous material for enantioselective separation and catalysis

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Contingent phosphorylation/dephosphorylation provides a mechanism of molecular memory in WASP.

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Phosphorylation of the WASP-VCA domain increases its affinity for the Arp2/3 complex and enhances actin polymerization by WASP

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The WASP-binding protein WIRE has a role in the regulation of the actin filament system downstream of the platelet-derived growth factor receptor

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WICH, a novel verprolin homology domain-containing protein that functions cooperatively with N-WASP in actin-microspike formation

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The WASp homologue Las17p functions with the WIP homologue End5p/verprolin and is essential for endocytosis in yeast

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WIP regulates N-WASP-mediated actin polymerization and filopodium formation

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A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization

1 reference

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The rat homologue of Wiskott-Aldrich syndrome protein (WASP)-interacting protein (WIP) associates with actin filaments, recruits N-WASP from the nucleus, and mediates mobilization of actin from stress fibers in favor of filopodia formation

1 reference

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WIP participates in actin reorganization and ruffle formation induced by PDGF

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PDGF alpha- and beta-receptors activate unique and common signal transduction pathways

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Structure of the N-WASP EVH1 Domain-WIP Complex

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Structural basis of Wiskott-Aldrich syndrome causing mutations in the WH1 domain

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The WH1 and EVH1 domains of WASP and Ena/VASP family members bind distinct sequence motifs

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Cortactin interacts with WIP in regulating Arp2/3 activation and membrane protrusion

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A WASp homolog powers actin polymerization-dependent motility of endosomes in vivo.

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Actin-dependent propulsion of endosomes and lysosomes by recruitment of N-WASP.

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Syndapins integrate N-WASP in receptor-mediated endocytosis.

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Neural Wiskott-Aldrich syndrome protein is recruited to rafts and associates with endophilin A in response to epidermal growth factor

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10.1016/J.YEXCR.2004.04.050

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