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

Miho Matsuda, Chih Wen Chu, Sergei Y. Sokol

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

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.

Original languageEnglish
Article numberdev200236
JournalDevelopment (Cambridge)
Volume149
Issue number10
DOIs
StatePublished - May 2022

Keywords

  • Actomyosin contractility
  • Adherens junctions
  • Lmo7
  • Morphogenesis
  • Non-muscle myosin II
  • Xenopus ectoderm

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