Nesprin-1 and nesprin-2 regulate endothelial cell shape and migration

Samantha J King, Karolin Nowak, Narendra Suryavanshi, Ian Holt, Catherine M Shanahan, Anne J Ridley

Research output: Contribution to journalArticle (Academic Journal)peer-review

27 Citations (Scopus)

Abstract

Nesprins are large multi-domain proteins that link the nuclear envelope to the cytoskeleton and nucleoskeleton. Here we show that nesprin-1 and nesprin-2 play important roles in regulating cell shape and migration in endothelial cells. Nesprin-1 or nesprin-2 depletion by RNAi increased endothelial cell spread area and the length of cellular protrusions, as well as stimulating stress fibre assembly which correlated with an increase in F-actin levels. Nuclear area was also increased by nesprin depletion, and localization of the inner nuclear membrane protein emerin to the nuclear envelope was reduced. Depletion of nesprin-1 or nesprin-2 reduced migration of endothelial cells into a cell-free area, and decreased loop formation in an in vitro angiogenesis assay. Taken together, our results indicate that nesprin-1 and nesprin-2 both regulate nuclear and cytoplasmic architecture, which we propose leads to their effects on endothelial cell migration and angiogenic loop formation.

Original languageEnglish
Pages (from-to)423-34
Number of pages12
JournalCytoskeleton (Hoboken, N.J.)
Volume71
Issue number7
DOIs
Publication statusPublished - Jul 2014

Keywords

  • Actins
  • Cell Movement
  • Cell Shape
  • Exons
  • Human Umbilical Vein Endothelial Cells
  • Humans
  • Membrane Proteins
  • Microfilament Proteins
  • Neovascularization, Physiologic
  • Nerve Tissue Proteins
  • Nuclear Envelope
  • Nuclear Proteins
  • Protein Transport
  • RNA, Small Interfering
  • Journal Article
  • Research Support, Non-U.S. Gov't

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