Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10871058 | FEBS Letters | 2013 | 8 Pages |
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 (nrp1cytoÎ/Î) 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 nrp1cytoÎ/Î ECs was an order of magnitude lower in comparison to nrp1+/+ ECs, thus accounting for the slower migration rate of the nrp1cytoÎ/Î ECs.
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Authors
Himabindu Reddy Seerapu, Susmita Borthakur, Nathan Kong, Sudesh Agrawal, Judy Drazba, Amit Vasanji, Alessandro Fantin, Christiana Ruhrberg, Matthias Buck, Arie Horowitz,