Expanding Actin Rings Zipper the Mouse Embryo for Blastocyst Formation

Cell. 2018 Apr 19;173(3):776-791.e17. doi: 10.1016/j.cell.2018.02.035. Epub 2018 Mar 22.

Abstract

Transformation from morula to blastocyst is a defining event of preimplantation embryo development. During this transition, the embryo must establish a paracellular permeability barrier to enable expansion of the blastocyst cavity. Here, using live imaging of mouse embryos, we reveal an actin-zippering mechanism driving this embryo sealing. Preceding blastocyst stage, a cortical F-actin ring assembles at the apical pole of the embryo's outer cells. The ring structure forms when cortical actin flows encounter a network of polar microtubules that exclude F-actin. Unlike stereotypical actin rings, the actin rings of the mouse embryo are not contractile, but instead, they expand to the cell-cell junctions. Here, they couple to the junctions by recruiting and stabilizing adherens and tight junction components. Coupling of the actin rings triggers localized myosin II accumulation, and it initiates a tension-dependent zippering mechanism along the junctions that is required to seal the embryo for blastocyst formation.

Keywords: actin dynamics; blastocyst; cortical flow; epithelia; live imaging; mammalian development; microtubules; morphogenesis; preimplantation mouse embryo; tight junctions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / chemistry*
  • Animals
  • Blastocyst / metabolism*
  • Cell Communication
  • Cytoskeletal Proteins / chemistry
  • Embryo, Mammalian
  • Embryonic Development
  • Female
  • Green Fluorescent Proteins
  • Imaging, Three-Dimensional
  • Mice
  • Mice, Inbred C57BL
  • Microtubules / metabolism*
  • Morula
  • Myosin Type II / chemistry*
  • RNA, Small Interfering / metabolism
  • Tight Junctions

Substances

  • Actins
  • Cytoskeletal Proteins
  • RNA, Small Interfering
  • Green Fluorescent Proteins
  • Myosin Type II