title: Abp1 utilizes the Arp2/3 complex activator Scar/WAVE in bristle development.
abstract: Many developmental processes rely on cortical actin dynamics; however, the mechanisms of its fine control at the cell cortex are still largely unknown. Our analyses demonstrate that the lipid- and F-actin-binding protein Abp1 is crucial for actin-driven bristle development in Drosophila melanogaster. Combined genetic, cell biological and biochemical analyses reveal that Abp1 triggers cortical Arp2/3-mediated actin nucleation by complex formation with Scar in bristle development. The role of the plasma-membrane-associated Abp1 subpool was highlighted by constitutively membrane-anchored Abp1. Such gain-of-function experiments led to a severe split-bristle phenotype, which was negatively correlated with bristle length. This phenotype was dependent on Scar but not on WASP and required the Scar-interacting SH3 domain of Abp1. Strikingly, knockout of abp1 led to defects in both microchaete and macrochaete bristle integrity. Importantly, Arp2- and Scar-deficient flies displayed similar bristle phenotypes. Microchaetes of flies deficient for Abp1, Arp2 and Scar functions had kinks, whereas those of wasp heterozygous flies did not. Electron microscopy analyses revealed that abp1 knockout, Arp2 RNAi and Scar RNAi all led to distorted macrochaetes with an excessive number of ridges. Interestingly, despite the physical association of Abp1 with Scar and its ability to use the Arp2/3 complex activator as an effector, abp1 knockout did not affect Scar stability. This is in contrast to classical Scar complex components, such as Kette or Sra-1. Our work reveals that Abp1 is an important, Scar-interacting factor controlling cortical Arp2/3-mediated actin nucleation and unravels a novel layer of complexity in the scrupulous control of cortical actin nucleation during sensory organ formation.
authors.affiliation: Institute for Biochemistry I, Jena University Hospital - Friedrich Schiller University Jena, 07743 Jena,  Germany.
authors.forename: Nicole
authors.initials: N
authors.lastname: Koch
authors.forename: Elavarasi
authors.initials: E
authors.lastname: Dharmalingam
authors.forename: Martin
authors.initials: M
authors.lastname: Westermann
authors.forename: Britta
authors.initials: B
authors.lastname: Qualmann
authors.forename: Ulrich
authors.initials: U
authors.lastname: Thomas
authors.forename: Michael M
authors.initials: MM
authors.lastname: Kessels
mesh_terms: D008841:Actin Cytoskeleton / Q000737:chemistry / Q000378:metabolism*; D051376:Actin-Related Protein 2-3 Complex / Q000235:genetics / Q000378:metabolism*; D000199:Actins / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D019556:COS Cells; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D002462:Cell Membrane / Q000235:genetics / Q000378:metabolism; D002522:Chlorocebus aethiops; D029721:Drosophila Proteins / Q000235:genetics / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000235:genetics / Q000254:growth & development* / Q000378:metabolism; D055786:Gene Knockout Techniques; D057809:HEK293 Cells; D006801:Humans; D008840:Microfilament Proteins / Q000172:deficiency / Q000235:genetics / Q000378:metabolism*; D034622:RNA Interference; D015398:Signal Transduction; D051300:Wiskott-Aldrich Syndrome Protein Family / Q000235:genetics / Q000378:metabolism*; D018909:src Homology Domains
chemical_list: D051376:Actin-Related Protein 2-3 Complex; D000199:Actins; D002352:Carrier Proteins; D029721:Drosophila Proteins; C034037:F-actin-binding proteins; D008840:Microfilament Proteins; C449671:SCAR protein, Drosophila; D051300:Wiskott-Aldrich Syndrome Protein Family; C478569:hem protein, Drosophila