title: Plexins function in epithelial repair in both Drosophila and zebrafish.
abstract: In most multicellular organisms, homeostasis is contingent upon maintaining epithelial integrity. When unanticipated insults breach epithelial barriers, dormant programmes of tissue repair are immediately activated. However, many of the mechanisms that repair damaged epithelia remain poorly characterized. Here we describe a role for Plexin A (PlexA), a protein with particularly well-characterized roles in axonal pathfinding, in the healing of damaged epithelia in Drosophila. Semaphorins, which are PlexA ligands, also regulate tissue repair. We show that Drosophila PlexA has GAP activity for the Rap1 GTPase, which is known to regulate the stability of adherens junctions. Our observations suggest that the inhibition of Rap1 activity by PlexA in damaged Drosophila epithelia allows epithelial remodelling, thus facilitating wound repair. We also demonstrate a role for Plexin A1, a zebrafish orthologue of Drosophila PlexA, in epithelial repair in zebrafish tail fins. Thus, plexins function in epithelial wound healing in diverse taxa.
authors.affiliation: Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA.|The Miller Institute, University of California, Berkeley, California 94720, USA.|Physiological Genetics Laboratory, RIKEN, 2-2-3 Minatojima-minamimachi, Chuo-ku, Kobe 650-0047, Japan.
authors.forename: Sa Kan
authors.initials: SK
authors.lastname: Yoo
authors.affiliation: Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA.
authors.forename: Heath G
authors.initials: HG
authors.lastname: Pascoe
authors.affiliation: Instituto de Medicina Molecular, Faculdade de Medicina da Universidade de Lisboa, 1649-028 Lisboa, Portugal.|CEDOC, Chronic Diseases Research Centre, NOVA Medical School, Universidade NOVA de Lisboa, 130, 1169-056 Lisboa, Portugal.
authors.forename: Telmo
authors.initials: T
authors.lastname: Pereira
authors.affiliation: Genetic Strains Research Center, National Institute of Genetics, 1111 Yata, Mishima, Shizuoka 411-8540, Japan.
authors.forename: Shu
authors.initials: S
authors.lastname: Kondo
authors.affiliation: CEDOC, Chronic Diseases Research Centre, NOVA Medical School, Universidade NOVA de Lisboa, 130, 1169-056 Lisboa, Portugal.
authors.forename: Antonio
authors.initials: A
authors.lastname: Jacinto
authors.affiliation: Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA.
authors.forename: Xuewu
authors.initials: X
authors.lastname: Zhang
authors.affiliation: Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA.
authors.forename: Iswar K
authors.initials: IK
authors.lastname: Hariharan
mesh_terms: D000199:Actins / Q000378:metabolism; D022005:Adherens Junctions / Q000378:metabolism; D058500:Animal Fins / Q000378:metabolism; D000818:Animals; D015815:Cell Adhesion Molecules / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000378:metabolism*; D004847:Epithelial Cells / Q000378:metabolism; D004848:Epithelium / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D034622:RNA Interference; D015398:Signal Transduction; D014945:Wound Healing; D015027:Zebrafish / Q000378:metabolism*
chemical_list: D000199:Actins; D015815:Cell Adhesion Molecules; D009419:Nerve Tissue Proteins; C091529:plexin