First Author | Seerapu HR | Year | 2013 |
Journal | FEBS Lett | Volume | 587 |
Issue | 21 | Pages | 3392-9 |
PubMed ID | 24021649 | Mgi Jnum | J:202477 |
Mgi Id | MGI:5519166 | Doi | 10.1016/j.febslet.2013.08.040 |
Citation | Seerapu HR, et al. (2013) The cytoplasmic domain of neuropilin-1 regulates focal adhesion turnover. FEBS Lett 587(21):3392-9 |
abstractText | 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)(Delta/Delta)) 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)(Delta/Delta) ECs was an order of magnitude lower in comparison to nrp1(+/+) ECs, thus accounting for the slower migration rate of the nrp1(cyto)(Delta/Delta) ECs. |