Rab35 controls actin bundling by recruiting fascin as an effector protein. Science (New York, N.Y.) [Science] Journal article

Title	Rab35 controls actin bundling by recruiting fascin as an effector protein.
Author(s)	Zhang J, Fonovic M, Suyama K, Bogyo M, Scott MP
Institution	Department of Developmental Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Source	Science 2009 Sep 4; 325(5945):1250-4.
MeSH	Actins Animals Carrier Proteins Cell Line Cell Membrane Drosophila Drosophila Proteins Hela Cells Humans Mice Microfilament Proteins Microfilaments Mitochondrial Membranes NIH 3T3 Cells Pseudopodia RNA Interference Recombinant Fusion Proteins rab GTP-Binding Proteins
Abstract	Actin filaments are key components of the eukaryotic cytoskeleton that provide mechanical structure and generate forces during cell shape changes, growth, and migration. Actin filaments are dynamically assembled into higher-order structures at specified locations to regulate diverse functions. The Rab family of small guanosine triphosphatases is evolutionarily conserved and mediates intracellular vesicle trafficking. We found that Rab35 regulates the assembly of actin filaments during bristle development in Drosophila and filopodia formation in cultured cells. These effects were mediated by the actin-bundling protein fascin, which directly associated with active Rab35. Targeting Rab35 to the outer mitochondrial membrane triggered actin recruitment, demonstrating a role for an intracellular trafficking protein in localized actin assembly.
Language	eng
Pub Type(s)	Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't
PubMed ID	19729655

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