A WASp-VASP complex regulates actin polymerization at the plasma membrane
نویسندگان
چکیده
منابع مشابه
How Wasp Regulates Actin Polymerization
Protrusion of lamellipodia and filopodia from the cell surface requires that actin polymerize locally. Actin polymerization is initiated by numerous agonists, including growth factors, chemoattractants, extracellular matrix, and phagocytic particles. The signaling pathways from the corresponding receptors converge on Rho family GTPases, especially Rac and Cdc42, which induce actin polymerizatio...
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Extended Fer-CIP4 homology (EFC)/FCH-BAR (F-BAR) domains generate and bind to tubular membrane structures of defined diameters that are involved in the formation and fission of endocytotic vesicles. Formin-binding protein 17 (FBP17) and Toca-1 contain EFC/F-BAR domains and bind to neural Wiskott-Aldrich syndrome protein (N-WASP), which links phosphatidylinositol (4,5)-bisphosphate (PIP(2)) and ...
متن کاملActin polymerization: Where the WASP stings
How do extracellular signals induce actin polymerization, as required for many cellular responses? Key signal transducers, such as the small GTPases Cdc42 and Rac, have now been shown to link via proteins of the WASP family to the Arp2/3 complex, which nucleates actin polymerization.
متن کاملCompetition between Blown fuse and WASP for WIP binding regulates the dynamics of WASP-dependent actin polymerization in vivo.
Dynamic rearrangements of the actin cytoskeleton play a key role in numerous cellular processes. In Drosophila, fusion between a muscle founder cell and a fusion competent myoblast (FCM) is mediated by an invasive, F-actin-enriched podosome-like structure (PLS). Here, we show that the dynamics of the PLS is controlled by Blown fuse (Blow), a cytoplasmic protein required for myoblast fusion but ...
متن کاملInducible recruitment of Cdc42 or WASP to a cell-surface receptor triggers actin polymerization and filopodium formation
BACKGROUND Cdc42, a GTP-binding protein of the Rho family, controls actin cytoskeletal organization and helps to generate actin-based protruding structures, such as filopodia. In vitro, Cdc42 regulates actin polymerization by facilitating the creation of free barbed ends - the more rapidly growing ends of actin filaments - and subsequent elongation at these ends. The Wiskott- Aldrich syndrome p...
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ژورنال
عنوان ژورنال: The EMBO Journal
سال: 2001
ISSN: 1460-2075
DOI: 10.1093/emboj/20.20.5603