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The cytoplasmic domain of neuropilin-1 regulates focal adhesion turnover

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
587
Issue
21
Identifiers
DOI: 10.1016/j.febslet.2013.08.040
Keywords
  • Neuropilin-1
  • Cytoplasmic Domain
  • Filamin A
  • Focal Adhesion

Abstract

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 (nrp1cytoΔ/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 nrp1cytoΔ/Δ ECs was an order of magnitude lower in comparison to nrp1+/+ ECs, thus accounting for the slower migration rate of the nrp1cytoΔ/Δ ECs.

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