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

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

SUBMITTER: Seerapu HR

PROVIDER: S-EPMC3856898 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature

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

Seerapu Himabindu Reddy HR Borthakur Susmita S Kong Nathan N Agrawal Sudesh S Drazba Judy J Vasanji Amit A Fantin Alessandro A Ruhrberg Christiana C Buck Matthias M Horowitz Arie A

FEBS letters 20130908 21

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 wil ...[more]

PMID: 24021649

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