The cytoplasmic domain of neuropilin-1 regulates focal adhesion turnover

FEBS Lett. 2013 Nov 1;587(21):3392-9. doi: 10.1016/j.febslet.2013.08.040. Epub 2013 Sep 8.

Abstract

Though the vascular endothelial growth factor coreceptor neuropilin-1 (Nrp1) plays a critical role in vascular development, its precise function is not fully understood. We identified a group of novel binding partners of the cytoplasmic domain of Nrp1 that includes the focal adhesion regulator, Filamin A (FlnA). Endothelial cells (ECs) expressing a Nrp1 mutant devoid of the cytoplasmic domain (nrp1(cyto)(Δ/Δ)) migrated significantly slower in response to VEGF relative to the cells expressing wild-type Nrp1 (nrp1(+/+) cells). The rate of FA turnover in VEGF-treated nrp1(cyto)(Δ/Δ) ECs was an order of magnitude lower in comparison to nrp1(+/+) ECs, thus accounting for the slower migration rate of the nrp1(cyto)(Δ/Δ) ECs.

Keywords: Cytoplasmic domain; Filamin A; Focal adhesion; Neuropilin-1.

Publication types

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

MeSH terms

  • Animals
  • Cell Adhesion
  • Cytoplasm / metabolism
  • Endothelium, Vascular / cytology
  • Endothelium, Vascular / metabolism
  • Filamins / chemistry
  • Filamins / metabolism
  • Focal Adhesions / metabolism*
  • Mice
  • Mutation
  • Neuropilin-1 / chemistry*
  • Neuropilin-1 / genetics
  • Neuropilin-1 / metabolism*
  • Signal Transduction
  • Vascular Endothelial Growth Factor A / genetics
  • Vascular Endothelial Growth Factor A / metabolism

Substances

  • Filamins
  • Vascular Endothelial Growth Factor A
  • Neuropilin-1