Role of nesprin-1 in nuclear deformation in endothelial cells under static and uniaxial stretching conditions

Biochem Biophys Res Commun. 2012 Jul 20;424(1):94-9. doi: 10.1016/j.bbrc.2012.06.073. Epub 2012 Jun 21.


The linker of nucleus and cytoskeleton (LINC) complex, including nesprin-1, has been suggested to be crucial for many biological processes. Previous studies have shown that mutations in nesprin-1 cause abnormal cellular functions and diseases, possibly because of insufficient force transmission to the nucleus through actin filaments (F-actin) bound to nesprin-1. However, little is known regarding the mechanical interaction between the nucleus and F-actin through nesprin-1. In this study, we examined nuclear deformation behavior in nesprin-1 knocked-down endothelial cells (ECs) subjected to uniaxial stretching by evaluating nuclear strain from lateral cross-sectional images. The widths of nuclei in nesprin-1 knocked-down ECs were smaller than those in wild-type cells. In addition, nuclear strain in nesprin-1 knocked-down cells, which is considered to be compressed by the actin cortical layer, increased compared with that in wild-type cells under stretching condition. These results indicate that nesprin-1 knockdown releases the nucleus from the tension of F-actin bound to the nucleus, thereby increasing allowance for deformation before stretching, and that F-actin bound to the nucleus through nesprin-1 causes sustainable force transmission to the nucleus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Cell Nucleus / physiology*
  • Cell Nucleus / ultrastructure*
  • Cells, Cultured
  • Cytoskeletal Proteins
  • Gene Knockdown Techniques
  • Human Umbilical Vein Endothelial Cells / metabolism
  • Human Umbilical Vein Endothelial Cells / physiology*
  • Human Umbilical Vein Endothelial Cells / ultrastructure
  • Humans
  • Mechanical Phenomena*
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism
  • Nerve Tissue Proteins / physiology*
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism
  • Nuclear Proteins / physiology*


  • Actins
  • Cytoskeletal Proteins
  • Nerve Tissue Proteins
  • Nuclear Proteins
  • SYNE1 protein, human