title: The Gas2 family protein Pigs is a microtubule +TIP that affects cytoskeleton organisation.
abstract: Coordination between different cytoskeletal systems is crucial for many cell biological functions, including cell migration and mitosis, and also plays an important role during tissue morphogenesis. Proteins of the class of cytoskeletal crosslinkers, or cytolinkers, have the ability to interact with more than one cytoskeletal system at a time and are prime candidates to mediate any coordination. One such class comprises the Gas2-like proteins, combining a conserved calponin-homology-type actin-binding domain and a Gas2 domain predicted to bind microtubules (MTs). This domain combination is also found in spectraplakins, huge cytolinkers that play important roles in many tissues in both invertebrates and vertebrates. Here, we dissect the ability of the single Drosophila Gas2-like protein Pigs to interact with both actin and MT cytoskeletons, both in vitro and in vivo, and illustrate complex regulatory interactions that determine the localisation of Pigs to and its effects on the cytoskeleton.
authors.affiliation: MRC-Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Avenue, Cambridge CB2 0QH, UK.
authors.forename: Gemma C
authors.initials: GC
authors.lastname: Girdler
authors.affiliation: Department of Biology & Carolina Center for Genome Sciences, The University of North Carolina at Chapel Hill, Campus Box 3280, 422 Fordham Hall, Chapel Hill, NC 27599-3280, USA Department of Biology, Reed College, 3203 SE Woodstock Boulevard, Portland, OR 97202, USA.
authors.forename: Derek A
authors.initials: DA
authors.lastname: Applewhite
authors.affiliation: Department of Biology, Reed College, 3203 SE Woodstock Boulevard, Portland, OR 97202, USA.
authors.forename: Wick M G
authors.initials: WM
authors.lastname: Perry
authors.affiliation: Department of Biology & Carolina Center for Genome Sciences, The University of North Carolina at Chapel Hill, Campus Box 3280, 422 Fordham Hall, Chapel Hill, NC 27599-3280, USA SRogers@bio.unc.edu kroeper@mrc-lmb.cam.ac.uk.
authors.forename: Stephen L
authors.initials: SL
authors.lastname: Rogers
authors.affiliation: MRC-Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Avenue, Cambridge CB2 0QH, UK SRogers@bio.unc.edu kroeper@mrc-lmb.cam.ac.uk.
authors.forename: Katja
authors.initials: K
authors.lastname: Röper
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism; D000199:Actins / Q000378:metabolism; D020816:Amino Acid Motifs; D000818:Animals; D016764:Cell Polarity; D002478:Cells, Cultured; D029721:Drosophila Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000378:metabolism*; D047908:Intracellular Signaling Peptides and Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism*; D009154:Mutation / Q000235:genetics; D011485:Protein Binding; D017434:Protein Structure, Tertiary
chemical_list: D000199:Actins; D029721:Drosophila Proteins; D047908:Intracellular Signaling Peptides and Proteins; C548372:Pigs protein, Drosophila
keywords: Actin; Cytolinker; Cytoskeleton; Drosophila; Gas2-like; Microtubule