title: The receptor-like tyrosine phosphatase lar is required for epithelial planar polarity and for axis determination within drosophila ovarian follicles.
abstract: The follicle cell monolayer that encircles each developing Drosophila oocyte contributes actively to egg development and patterning, and also represents a model stem cell-derived epithelium. We have identified mutations in the receptor-like transmembrane tyrosine phosphatase Lar that disorganize follicle formation, block egg chamber elongation and disrupt Oskar localization, which is an indicator of oocyte anterior-posterior polarity. Alterations in actin filament organization correlate with these defects. Actin filaments in the basal follicle cell domain normally become polarized during stage 6 around the anterior-posterior axis defined by the polar cells, but mutations in Lar frequently disrupt polar cell differentiation and actin polarization. Lar function is only needed in somatic cells, and (for Oskar localization) its action is autonomous to posterior follicle cells. Polarity signals may be laid down by these cells within the extracellular matrix (ECM), possibly in the distribution of the candidate Lar ligand Laminin A, and read out at the time Oskar is localized in a Lar-dependent manner. Lar is not required autonomously to polarize somatic cell actin during stages 6. We show that Lar acts somatically early in oogenesis, during follicle formation, and postulate that it functions in germarium intercyst cells that are required for polar cell specification and differentiation. Our studies suggest that positional information can be stored transiently in the ECM. A major function of Lar may be to transduce such signals.
authors.affiliation: Howard Hughes Medical Institute, Department of Embryology, Carnegie Institution of Washington, Baltimore, MD 21210, USA.
authors.forename: H M
authors.initials: HM
authors.lastname: Frydman
authors.forename: A C
authors.initials: AC
authors.lastname: Spradling
mesh_terms: D000199:Actins / Q000378:metabolism; D000483:Alleles; D000818:Animals; D015152:Blotting, Northern; D019521:Body Patterning; D002454:Cell Differentiation; D004330:Drosophila; D004848:Epithelium / Q000196:embryology*; D005109:Extracellular Matrix / Q000378:metabolism; D005260:Female; D017403:In Situ Hybridization; D007247:Infertility, Female; D007797:Laminin / Q000378:metabolism; D008855:Microscopy, Electron, Scanning; D008856:Microscopy, Fluorescence; D008953:Models, Anatomic; D008954:Models, Biological; D009154:Mutation; D006080:Ovarian Follicle / Q000196:embryology* / Q000378:metabolism; D010053:Ovary / Q000196:embryology*; D017027:Protein Tyrosine Phosphatases / Q000378:metabolism* / Q000502:physiology*; D054630:Receptor-Like Protein Tyrosine Phosphatases, Class 4; D011956:Receptors, Cell Surface; D015398:Signal Transduction
chemical_list: D000199:Actins; D007797:Laminin; D011956:Receptors, Cell Surface; C084098:laminin A; D017027:Protein Tyrosine Phosphatases; D054630:Receptor-Like Protein Tyrosine Phosphatases, Class 4