Spatiotemporal control of epithelial remodeling by regulated myosin phosphorylation Journal Article


Authors: Kasza, K. E.; Farrell, D. L.; Zallen, J. A.
Article Title: Spatiotemporal control of epithelial remodeling by regulated myosin phosphorylation
Abstract: Spatiotemporally regulated actomyosin contractility generates the forces that drive epithelial cell rearrangements and tissue remodeling. Phosphorylation of the myosin II regulatory light chain (RLC) promotes the assembly of myosin monomers into active contractile filaments and is an essential mechanism regulating the level of myosin activity. However, the effects of phosphorylation on myosin localization, dynamics, and function during epithelial remodeling are not well understood. In Drosophila, planar polarized myosin contractility is required for oriented cell rearrangements during elongation of the body axis. We show that regulated myosin phosphorylation influences spatial and temporal properties of contractile behavior at molecular, cellular, and tissue length scales. Expression of myosin RLC variants that prevent or mimic phosphorylation both disrupt axis elongation, but have distinct effects at the molecular and cellular levels. Unphosphorylatable RLC produces fewer, slower cell rearrangements, whereas phosphomimetic RLC accelerates rearrangement and promotes higher-order cell interactions. Quantitative live imaging and biophysical approaches reveal that both phosphovariants reduce myosin planar polarity and mechanical anisotropy, altering the orientation of cell rearrangements during axis elongation. Moreover, the localized myosin activator Rho-kinase is required for spatially regulated myosin activity, even when the requirement for phosphorylation is bypassed by the expression of phosphomimetic myosin RLC. These results indicate that myosin phosphorylation influences both the level and the spatiotemporal regulation of myosin activity, linking molecular properties of myosin activity to tissue morphogenesis.
Keywords: controlled study; protein phosphorylation; nonhuman; protein localization; cell function; embryo; drosophila; cell interaction; myosin; myosin adenosine triphosphatase; myosin ii; anisotropy; rho kinase; priority journal; article
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 111
Issue: 32
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 2014-08-12
Start Page: 11732
End Page: 11737
Language: English
DOI: 10.1073/pnas.1400520111
PROVIDER: scopus
PMCID: PMC4136583
PUBMED: 25071215
DOI/URL:
Notes: Cited By (since 1996):1 -- Export Date: 2 September 2014 -- CODEN: PNASA -- Source: Scopus
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MSK Authors
  1. Jennifer A Zallen
    39 Zallen
  2. Karen E Kasza
    3 Kasza