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VEGFA activates NRP1. 18 / 30
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"Since GIPC1 interacts with neuropilin-1 XREF_BIBR, cells were treated with VEGFA (10 ng/ml) to determine whether the loss of cell viability caused by GIPC1 suppression could be overcome by a relevant mitogen."
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"VEGFR-1, but not VEGFR-2, is expressed in motor neurons of the facial nerve, leading to the assumption that VEGF-A induces the formation of a complex of VEGFR-1 and Nrp-1 that then transmits the VEGF-A signal [XREF_BIBR]."
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"VEGF-A addition also increased the number of microspikes in NRP1 depleted ECs on FN (XREF_FIG L, compare light gray columns)."
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"In the absence of VEGFR-2, NRP-1 can still be activated by VEGF-A."
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"NRP-1 can be activated by VEGF-A also in the absence of VEGFRs, triggering specific signal transduction pathways (e.g. p130Cas phosphorylation)."
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"Concomitantly, VEGF-A-dependent activation of Neuropilin-1 (NRP-1) in the tip cells inhibits SMAD2/3 and SMAD1/5/8 signaling ultimately repressing the stalk cell phenotype and maintaining tip cell identity [ xref ]."
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"This binding strongly inhibits the activation of NRP-1 by VEGF-A 165 , and the LPPR sequence is responsible for 75% of this inhibition [ xref ]."
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"VEGF-A 165 promotes the formation of a complex of NRP1 and KDR in endothelial cells, which is thought to be important for optimal VEGF signaling and function."
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"Unlike sema3C treated ECs, Nrp1 did not colocalize with CTbeta in cells treated with VEGF-A 165 (XREF_SUPPLEMENTARY and XREF_FIG)."
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"In addition, recent studies of the VEGFR co-receptor neuropilin-1 (Nrp-1) have shown that the C terminus of VEGF-A 165, particularly Arg 164, mediates high affinity binding of Nrp-1, increasing VEGFR activity [XREF_BIBR]."
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"Concomitantly, VEGFA-dependent activation of Neuropilin-1 (NRP-1) in the tip cells inhibits SMAD2/3 and SMAD1/5/8 signaling ultimately repressing the stalk cell phenotype and maintaining tip cell identity [21]."
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"As a consequence, VEGF-A induced NRP1 and GIPC1 and GIPC1 and Syx complex formation without the expression of VEGFR1 or VEGFR2."
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"VEGFA 165 induces association of Nrp1, VEGFR2, and synectin to form a protein complex and drive intracellular trafficking of Nrp1 and VEGFR2 through specific endosomal compartments."
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"Both studies demonstrate that VEGF-A promotes axon guidance independently of its vascular roles through two receptors, either VEGFR2 (Ruiz de Almodovar et al., 2011) or neuropilin-1 (NRP1) (Erskine et al., 2011)."
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"However, recent biochemical studies demonstrated that Sema3A and VEGF-A bind to distinct domains of NRP1 [XREF_BIBR, XREF_BIBR] and induce NRP1 endocytosis through different pathways, suggesting that these NRP1 ligands function separately, rather than competitively."
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"Moreover, it is not yet clear how the VEGF- and ECM driven NRP1 pathways described above intersect with NRP1 mediated TGFbeta signalling, discussed in the next section."
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"In the absence of VEGFR-2, NRP-1 can still be activated by VEGF-A. Expression of NRP-1 in melanoma cells correlates with tumour cell invasive behaviour and formation of tube-like structures resembling vascular networks (vasculogenic mimicry)."
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"As shown in Figure XREF_FIG, VEGF-A rapidly induced complex formation of NRP-1 and VEGFR2 in HUVECs."
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