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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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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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 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

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10.1016/J.YEXCR.2004.04.050

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