α-Spectrin and integrins act together to regulate actomyosin and columnarization, and to maintain a monolayered follicular epithelium

The spectrin cytoskeleton crosslinks actin to the membrane, and although it has been greatly studied in erythrocytes, much is unknown about its function in epithelia. We have studied the role of spectrins during epithelia morphogenesis using the Drosophila follicular epithelium (FE). As previously d...

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Published inDevelopment (Cambridge) Vol. 143; no. 8; pp. 1388 - 1399
Main Authors Ng, Bing Fu, Selvaraj, Gokul Kannan, Santa-Cruz Mateos, Carmen, Grosheva, Inna, Alvarez-Garcia, Ines, Martín-Bermudo, María Dolores, Palacios, Isabel M
Format Journal Article
LanguageEnglish
Published England The Company of Biologists Ltd 15.04.2016
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Summary:The spectrin cytoskeleton crosslinks actin to the membrane, and although it has been greatly studied in erythrocytes, much is unknown about its function in epithelia. We have studied the role of spectrins during epithelia morphogenesis using the Drosophila follicular epithelium (FE). As previously described, we show that α-Spectrin and β-Spectrin are essential to maintain a monolayered FE, but, contrary to previous work, spectrins are not required to control proliferation. Furthermore, spectrin mutant cells show differentiation and polarity defects only in the ectopic layers of stratified epithelia, similar to integrin mutants. Our results identify α-Spectrin and integrins as novel regulators of apical constriction-independent cell elongation, as α-Spectrin and integrin mutant cells fail to columnarize. Finally, we show that increasing and reducing the activity of the Rho1-Myosin II pathway enhances and decreases multilayering of α-Spectrin cells, respectively. Similarly, higher Myosin II activity enhances the integrin multilayering phenotype. This work identifies a primary role for α-Spectrin in controlling cell shape, perhaps by modulating actomyosin. In summary, we suggest that a functional spectrin-integrin complex is essential to balance adequate forces, in order to maintain a monolayered epithelium.
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Present address: PLOS Biology, Carlyle Road, Cambridge CB4 3DN, UK.
These authors contributed equally to this work
ISSN:0950-1991
1477-9129
DOI:10.1242/dev.130070