Drosophila Myosin II, Zipper, is essential for ommatidial rotation.
The adult Drosophila retina is a highly polarized epithelium derived from a precursor tissue that is initially symmetric across its dorsoventral axis. Specialized 90 degrees rotational movements of subsets of cells, the ommatidial precursors, establish mirror symmetry in the retinal epithelium. Myosin II, or Zipper (Zip), a motor protein, regulates the rate at which ommatidia rotate: in zip mutants, the rate of rotation is significantly slowed. Zip is concentrated in the cells that we show to be at the likely interface between rotating and non-rotating cells: the boundary between differentiated and undifferentiated cells. Zip is also robust in newly added ommatidial cells, consistent with our model that the machinery that drives rotation should shift to newly recruited cells as they are added to the growing ommatidium. Finally, cell death genes and canonical Wnt signaling pathway members genetically modify the zip phenotype.
Fiehler
Ryan W
RW
Department of Genetics, Washington University School of Medicine, St Louis, MO 63110, USA.
Wolff
Tanya
T
D000818:Animals; D002454:Cell Differentiation; D002465:Cell Movement; D004330:Drosophila / Q000166:cytology* / Q000254:growth & development; D029721:Drosophila Proteins / Q000235:genetics / Q000502:physiology*; D008565:Membrane Proteins / Q000235:genetics / Q000502:physiology*; D009154:Mutation; D018995:Myosin Heavy Chains / Q000235:genetics / Q000502:physiology*; D017956:Photoreceptor Cells, Invertebrate / Q000502:physiology; D012160:Retina / Q000166:cytology / Q000254:growth & development / Q000502:physiology*; D015398:Signal Transduction; D051153:Wnt Proteins / Q000378:metabolism