title: The lamellipodium: where motility begins.
abstract: Lamellipodia, filopodia and membrane ruffles are essential for cell motility, the organization of membrane domains, phagocytosis and the development of substrate adhesions. Their formation relies on the regulated recruitment of molecular scaffolds to their tips (to harness and localize actin polymerization), coupled to the coordinated organization of actin filaments into lamella networks and bundled arrays. Their turnover requires further molecular complexes for the disassembly and recycling of lamellipodium components. Here, we give a spatial inventory of the many molecular players in this dynamic domain of the actin cytoskeleton in order to highlight the open questions and the challenges ahead.
authors.affiliation: Dept of Cell Biology, Institute of Molecular Biology, Austrian Academy of Sciences, Billrothstrasse 11, 5020 Salzburg, Austria. jvsmall@imb.oeaw.ac.at
authors.forename: J Victor
authors.initials: JV
authors.lastname: Small
authors.forename: Theresia
authors.initials: T
authors.lastname: Stradal
authors.forename: Emmanuel
authors.initials: E
authors.lastname: Vignal
authors.forename: Klemens
authors.initials: K
authors.lastname: Rottner
mesh_terms: D000199:Actins / Q000378:metabolism; D000818:Animals; D002465:Cell Movement / Q000502:physiology; D046911:Macromolecular Substances; D020409:Molecular Motor Proteins / Q000737:chemistry / Q000502:physiology; D011506:Proteins; D011554:Pseudopodia / Q000737:chemistry* / Q000502:physiology / Q000648:ultrastructure; D015398:Signal Transduction; D020741:rho GTP-Binding Proteins / Q000502:physiology
chemical_list: D000199:Actins; D046911:Macromolecular Substances; D020409:Molecular Motor Proteins; D011506:Proteins; D020741:rho GTP-Binding Proteins