Cell-fibronectin interactions propel vertebrate trunk elongation via tissue mechanics

Curr Biol. 2013 Jul 22;23(14):1335-41. doi: 10.1016/j.cub.2013.05.052. Epub 2013 Jun 27.


During embryonic development and tissue homeostasis, cells produce and remodel the extracellular matrix (ECM). The ECM maintains tissue integrity and can serve as a substrate for cell migration. Integrin α5 (Itgα5) and αV (ItgαV) are the α subunits of the integrins most responsible for both cell adhesion to the ECM protein fibronectin (FN) and FN matrix fibrillogenesis. We perform a systems-level analysis of cell motion in the zebrafish tail bud during trunk elongation in the presence and absence of normal cell-FN interactions. Itgα5 and ItgαV have well-described roles in cell migration in vitro. However, we find that concomitant loss of itgα5 and itgαV leads to a trunk elongation defect without substantive alteration of cell migration. Tissue-specific transgenic rescue experiments suggest that the FN matrix on the surface of the paraxial mesoderm is required for body elongation via its role in defining tissue mechanics and intertissue adhesion.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Cell Adhesion
  • Cell Movement
  • Embryo, Nonmammalian / embryology
  • Embryo, Nonmammalian / metabolism
  • Extracellular Matrix / metabolism
  • Fibronectins / genetics*
  • Fibronectins / metabolism
  • Integrin alpha5 / genetics
  • Integrin alpha5 / metabolism
  • Integrin alphaV / genetics
  • Integrin alphaV / metabolism
  • Tail / embryology
  • Tail / metabolism
  • Zebrafish / embryology*
  • Zebrafish / genetics
  • Zebrafish / physiology*
  • Zebrafish Proteins / genetics*
  • Zebrafish Proteins / metabolism


  • Fibronectins
  • Integrin alpha5
  • Integrin alphaV
  • Zebrafish Proteins