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

The cytoplasmic domain of neuropilin-1 regulates focal adhesion turnover.
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DOI:
10.1016/j.febslet.2013.08.040
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发表时间:
2013-11-01
期刊:
影响因子:
3.5
通讯作者:
Horowitz A
Horowitz A
中科院分区:
生物学3区
文献类型:
--
作者:
Seerapu HR;Borthakur S;Kong N;Agrawal S;Drazba J;Vasanji A;Fantin A;Ruhrberg C;Buck M;Horowitz A

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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 protein FlnA. Endothelial cells (ECs) expressing a Nrp1 mutant devoid of a cytoplasmic domain (nrp1cytoΔ/Δ) instead of wild type Nrp1 migrated significantly slower in response to VEGF relative to 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.
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