Apical domain polarization localizes actin–myosin activity to drive ratchet-like apical constriction
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Mason et al 2013 Combined Document.pdf
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Author(s)
Tworoger, Michael B.
Martin, Adam C
Mason, Frank M
Date Issued
July 2013
Journal
Nature Cell Biology
Publisher
Nature Publishing Group
Citation
Mason, Frank M., Michael Tworoger, and Adam C. Martin. “Apical Domain Polarization Localizes Actin–myosin Activity to Drive Ratchet-Like Apical Constriction.” Nature Cell Biology 15, no. 8 (July 7, 2013): 926–936.
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Author's final manuscript
Abstract
Apical constriction promotes epithelia folding, which changes tissue architecture. During Drosophila gastrulation, mesoderm cells exhibit repeated contractile pulses that are stabilized such that cells apically constrict like a ratchet. The transcription factor Twist is required to stabilize cell shape. However, it is unknown how Twist spatially coordinates downstream signals to prevent cell relaxation. We find that during constriction, Rho-associated kinase (Rok) is polarized to the middle of the apical domain (medioapical cortex), separate from adherens junctions. Rok recruits or stabilizes medioapical myosin II (Myo-II), which contracts dynamic medioapical actin cables. The formin Diaphanous mediates apical actin assembly to suppress medioapical E-cadherin localization and form stable connections between the medioapical contractile network and adherens junctions. Twist is not required for apical Rok recruitment, but instead polarizes Rok medioapically. Therefore, Twist establishes radial cell polarity of Rok/Myo-II and E-cadherin and promotes medioapical actin assembly in mesoderm cells to stabilize cell shape fluctuations.
MIT Department
Massachusetts Institute of Technology. Department of Biology
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DOI of Published Version
https://doi.org/10.1038/ncb2796
