Lmo7 recruits myosin II heavy chain to regulate actomyosin contractility and apical domain size in Xenopus ectoderm

Development. 2022 May 15;149(10):dev200236. doi: 10.1242/dev.200236. Epub 2022 May 16.

Abstract

Apical constriction, or a reduction in size of the apical domain, underlies many morphogenetic events during development. Actomyosin complexes play an essential role in apical constriction; however, the detailed analysis of molecular mechanisms is still pending. Here, we show that Lim domain only protein 7 (Lmo7), a multidomain adaptor at apical junctions, promotes apical constriction in the Xenopus superficial ectoderm, whereas apical domain size increases in Lmo7-depleted cells. Lmo7 is primarily localized at apical junctions and promotes the formation of the dense circumferential actomyosin belt. Strikingly, Lmo7 binds non-muscle myosin II (NMII) and recruits it to apical junctions and the apical cortex. This NMII recruitment is essential for Lmo7-mediated apical constriction. Lmo7 knockdown decreases NMIIA localization at apical junctions and delays neural tube closure in Xenopus embryos. Our findings suggest that Lmo7 serves as a scaffold that regulates actomyosin contractility and apical domain size.

Keywords: Xenopus ectoderm; Actomyosin contractility; Adherens junctions; Lmo7; Morphogenesis; Non-muscle myosin II.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Actomyosin* / metabolism
  • Animals
  • Ectoderm* / metabolism
  • Morphogenesis / physiology
  • Myosin Heavy Chains
  • Myosin Type II / genetics
  • Myosin Type II / metabolism
  • Xenopus laevis / metabolism

Substances

  • Actomyosin
  • Myosin Type II
  • Myosin Heavy Chains