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

The cytoplasmic domain of neuropilin-1 regulates focal adhesion turnover.

Author information

1
Department of Molecular Cardiology, Lerner Research Institute, the Cleveland Clinic, Cleveland, OH 44195, United States.

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

PMID:
24021649
PMCID:
PMC3856898
DOI:
10.1016/j.febslet.2013.08.040
[Indexed for MEDLINE]
Free PMC Article

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