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Morphogenesis in Drosophila requires nonmuscle myosin heavy chain function
P E Young1, A M Richman, A S Ketchum
1Department of Cellular and Developmental Biology, Harvard Biological Laboratories, Harvard University, Cambridge, Massachusetts 02138.
Genes & Development
|January 1, 1993
Summary
This study links myosin II, a molecular motor, to morphogenesis, the process of cell shape change during development. Myosin II is essential for embryonic development, impacting cell shape and movement.
Area of Science:
- Developmental Biology
- Cell Biology
- Molecular Genetics
Background:
- Morphogenesis, essential for embryonic development, involves complex cell shape changes and movements.
- Molecular motors play critical roles in cellular processes, but their direct link to morphogenesis has been unclear.
Purpose of the Study:
- To establish the first direct link between a molecular motor and morphogenesis.
- To identify the gene product responsible for the embryonic-lethal 'zipper' mutations in Drosophila.
- To elucidate the role of nonmuscle myosin II in embryonic development.
Main Methods:
- Utilizing reverse genetics to create mutations in the Drosophila nonmuscle myosin II heavy chain gene.
- Allelic analysis to correlate mutations with previously identified 'zipper' mutations.
- Microscopic analysis of cell morphology and myosin localization in wild-type and mutant embryos.
Main Results:
- Mutations in the nonmuscle myosin II heavy chain gene are embryonic-lethal and allelic to 'zipper' mutations.
- Embryos lacking functional myosin II exhibit defects in dorsal closure, head involution, and axon patterning.
- Myosin II is crucial for maintaining cell shape and facilitates cell sheet movement during morphogenesis.
Conclusions:
- Nonmuscle myosin II is the product of the 'zipper' gene and is essential for Drosophila embryonic development.
- Myosin II plays a fundamental role in cell shape maintenance and cell sheet movement during morphogenesis.
- The processes of cell shape change in morphogenesis and cell division are mechanistically related, both requiring myosin.