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The cytoplasmic domain of neuropilin-1 regulates focal adhesion turnover |
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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 |
| Affiliation: | 1. Department of Molecular Cardiology, Lerner Research Institute, the Cleveland Clinic, Cleveland, OH 44195, United States;2. The Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH 44106, United States;3. Imaging Core Facility, Lerner Research Institute, the Cleveland Clinic, Cleveland, OH 44195, United States;4. Image-IQ, Cleveland, OH 44106, United States;5. University College London, Institute of Ophthalmology, London, UK |
| 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. |
| Keywords: | Neuropilin-1 Cytoplasmic domain Filamin A Focal adhesion |
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