4.4 Article

Drosophila Myosin II, Zipper, is essential for ommatidial rotation

Journal

DEVELOPMENTAL BIOLOGY
Volume 310, Issue 2, Pages 348-362

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ydbio.2007.08.001

Keywords

Zipper; Myosin II; ommatidial rotation; ommatidial orientation; Drosophila eye development; cell movements; cell death

Funding

  1. NEI NIH HHS [R01 EY013136-01, T32 EY013360, R01 EY013136-04, R01 EY013136-03, R01 EY013136-02, 5 T32 EY13360-05, R01 EY13136, R01 EY013136] Funding Source: Medline

Ask authors/readers for more resources

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 11, 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. Published by Elsevier Inc.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.4
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available