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Mutations in Drosophila crinkled/Myosin VIIA disrupt denticle morphogenesis.
- Source :
-
Developmental biology [Dev Biol] 2021 Feb; Vol. 470, pp. 121-135. Date of Electronic Publication: 2020 Nov 25. - Publication Year :
- 2021
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Abstract
- Actin filament crosslinking, bundling and molecular motor proteins are necessary for the assembly of epithelial projections such as microvilli, stereocilia, hairs, and bristles. Mutations in such proteins cause defects in the shape, structure, and function of these actin - based protrusions. One protein necessary for stereocilia formation, Myosin VIIA, is an actin - based motor protein conserved throughout phylogeny. In Drosophila melanogaster, severe mutations in the MyoVIIA homolog crinkled (ck) are "semi - lethal" with only a very small percentage of flies surviving to adulthood. Such survivors show morphological defects related to actin bundling in hairs and bristles. To better understand ck/MyoVIIA's function in bundled - actin structures, we used dominant female sterile approaches to analyze the loss of maternal and zygotic (M/Z) ck/MyoVIIA in the morphogenesis of denticles, small actin - based projections on the ventral epidermis of Drosophila embryos. M/Z ck mutants displayed severe defects in denticle morphology - actin filaments initiated in the correct location, but failed to elongate and bundle to form normal projections. Using deletion mutant constructs, we demonstrated that both of the C - terminal MyTH4 and FERM domains are necessary for proper denticle formation. Furthermore, we show that ck/MyoVIIA interacts genetically with dusky - like (dyl), a member of the ZPD family of proteins that links the extracellular matrix to the plasma membrane, and when mutated also disrupts normal denticle formation. Loss of either protein alone does not alter the localization of the other; however, loss of the two proteins together dramatically enhances the defects in denticle shape observed when either protein alone was absent. Our data indicate that ck/MyoVIIA plays a key role in the formation and/or organization of actin filament bundles, which drive proper shape of cellular projections.<br />Competing Interests: Declaration of competing interest Authors declare no competing financial interests.<br /> (Copyright © 2020 Elsevier Inc. All rights reserved.)
- Subjects :
- Actin Cytoskeleton metabolism
Animals
Drosophila Proteins genetics
Drosophila melanogaster metabolism
Epidermis embryology
Female
Male
Membrane Proteins genetics
Membrane Proteins metabolism
Morphogenesis
Mutant Proteins metabolism
Mutation
Myosin VIIa genetics
Actin Cytoskeleton ultrastructure
Cell Surface Extensions ultrastructure
Drosophila Proteins metabolism
Drosophila melanogaster embryology
Myosin VIIa metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1095-564X
- Volume :
- 470
- Database :
- MEDLINE
- Journal :
- Developmental biology
- Publication Type :
- Academic Journal
- Accession number :
- 33248112
- Full Text :
- https://doi.org/10.1016/j.ydbio.2020.11.007