title: Extending the Arp2/3 complex and its regulation beyond the leading edge.
abstract: Two studies characterizing Drosophila Arp2/3 complex and Scar mutants demonstrate that assembly of some actin structures in nonmotile cells of multicellular organisms utilizes the same proteins as are important for actin assembly in motile cells. These studies also show that assembly of other actin structures is independent of these proteins, suggesting that alternative mechanisms also exist.
authors.affiliation: Department of Biology, Washington University, St. Louis, MO 63130, USA. miller@biology.wustl.edu
authors.forename: Kathryn G
authors.initials: KG
authors.lastname: Miller
mesh_terms: D000818:Animals; D006801:Humans; D051377:Actin-Related Protein 2; D051378:Actin-Related Protein 3; D000199:Actins / Q000235:genetics / Q000378:metabolism; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism; D003598:Cytoskeletal Proteins; D004330:Drosophila / Q000196:embryology; D011506:Proteins / Q000235:genetics / Q000378:metabolism; D051316:Wiskott-Aldrich Syndrome Protein; D051300:Wiskott-Aldrich Syndrome Protein Family
chemical_list: D051377:Actin-Related Protein 2; D051378:Actin-Related Protein 3; D000199:Actins; C495926:ACTR2 protein, human; C495928:ACTR3 protein, human; D002352:Carrier Proteins; D003598:Cytoskeletal Proteins; D011506:Proteins; C495767:WAS protein, human; C114864:WASF1 protein, human; D051316:Wiskott-Aldrich Syndrome Protein; D051300:Wiskott-Aldrich Syndrome Protein Family