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NRP1 — VEGFA

Pathways - manually collected, often from reviews:

• NCI Pathway Database VEGF and VEGFR signaling network: VEGFR2 (dimer)/VEGFA (dimer)/NRP1 complex (KDR-VEGFA-NRP1) → VEGFA (dimer) complex (VEGFA) (modification, collaborate)
  Whitaker et al., J Biol Chem 2001*, Soker et al., J Cell Biochem 2002*, Mamluk et al., J Biol Chem 2002, Shintani et al., EMBO J 2006*, Prahst et al., J Biol Chem 2008*, Kawamura et al., Blood 2008*, Evans et al., Mol Cell Biol 2011*, Ballmer-Hofer et al., Blood 2011*
  Evidence: physical interaction
• NCI Pathway Database VEGF and VEGFR signaling network: VEGFR2 (dimer)/VEGFA (dimer)/NRP1 complex (KDR-VEGFA-NRP1) → NRP1 (NRP1) (modification, collaborate) Whitaker et al., J Biol Chem 2001*, Soker et al., J Cell Biochem 2002*, Mamluk et al., J Biol Chem 2002, Shintani et al., EMBO J 2006*, Prahst et al., J Biol Chem 2008*, Kawamura et al., Blood 2008*, Evans et al., Mol Cell Biol 2011*, Ballmer-Hofer et al., Blood 2011*
  Evidence: physical interaction
• NCI Pathway Database VEGF and VEGFR signaling network: VEGFR2 (dimer)/VEGFA (dimer)/NRP1 complex (KDR-VEGFA-NRP1) → VEGFR2 (KDR) (modification, collaborate) Whitaker et al., J Biol Chem 2001*, Soker et al., J Cell Biochem 2002*, Mamluk et al., J Biol Chem 2002, Shintani et al., EMBO J 2006*, Prahst et al., J Biol Chem 2008*, Kawamura et al., Blood 2008*, Evans et al., Mol Cell Biol 2011*, Ballmer-Hofer et al., Blood 2011*
  Evidence: physical interaction
• NCI Pathway Database VEGF and VEGFR signaling network: VEGFA (dimer) complex (VEGFA) → NRP1 (NRP1) (modification, collaborate) Whitaker et al., J Biol Chem 2001*, Soker et al., J Cell Biochem 2002*, Mamluk et al., J Biol Chem 2002, Shintani et al., EMBO J 2006*, Prahst et al., J Biol Chem 2008*, Kawamura et al., Blood 2008*, Evans et al., Mol Cell Biol 2011*, Ballmer-Hofer et al., Blood 2011*
  Evidence: physical interaction
• NCI Pathway Database VEGFR1 specific signals: VEGFR1 homodimer/NRP1/VEGFR 121 complex (FLT1-NRP1-VEGFA) → VEGFR1 homodimer/NRP1 complex (FLT1-NRP1) (modification, collaborate)
  Mamluk et al., J Biol Chem 2002
  Evidence: physical interaction
• NCI Pathway Database VEGFR1 specific signals: VEGFR1 homodimer/NRP1/VEGFR 121 complex (FLT1-NRP1-VEGFA) → VEGFA121 (VEGFA) (modification, collaborate) Mamluk et al., J Biol Chem 2002
  Evidence: physical interaction
• NCI Pathway Database VEGFR1 specific signals: VEGFR1 homodimer/NRP1 complex (FLT1-NRP1) → VEGFA121 (VEGFA) (modification, collaborate) Mamluk et al., J Biol Chem 2002
  Evidence: physical interaction
• NCI Pathway Database VEGF and VEGFR signaling network: VEGFR1 (dimer)/VEGFA (dimer)/NRP1 complex (FLT1-VEGFA-NRP1) → VEGFA (dimer) complex (VEGFA) (modification, collaborate)
  Fuh et al., J Biol Chem 2000*, Banerjee et al., Biochemistry 2008*, Kawamura et al., Blood 2008*
  Evidence: physical interaction
• NCI Pathway Database VEGF and VEGFR signaling network: VEGFR1 (dimer)/VEGFA (dimer)/NRP1 complex (FLT1-VEGFA-NRP1) → NRP1 (NRP1) (modification, collaborate) Fuh et al., J Biol Chem 2000*, Banerjee et al., Biochemistry 2008*, Kawamura et al., Blood 2008*
  Evidence: physical interaction
• NCI Pathway Database VEGF and VEGFR signaling network: VEGFR1 (dimer)/VEGFA (dimer)/NRP1 complex (FLT1-VEGFA-NRP1) → VEGFR1 (FLT1) (modification, collaborate) Fuh et al., J Biol Chem 2000*, Banerjee et al., Biochemistry 2008*, Kawamura et al., Blood 2008*
  Evidence: physical interaction
• NCI Pathway Database VEGF and VEGFR signaling network: VEGFA (dimer) complex (VEGFA) → NRP1 (NRP1) (modification, collaborate) Fuh et al., J Biol Chem 2000*, Banerjee et al., Biochemistry 2008*, Kawamura et al., Blood 2008*
  Evidence: physical interaction

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Bind_translation Interaction: NRP1 — VEGFA (competition binding) Mamluk et al., J Biol Chem 2002
• IRef Bind_translation Interaction: NRP1 — VEGFA (coimmunoprecipitation) Mamluk et al., J Biol Chem 2002
• IRef Bind_translation Interaction: NRP1 — VEGFA (cross-linking study) Mamluk et al., J Biol Chem 2002
• IRef Bind_translation Interaction: NRP1 — VEGFA (surface plasmon resonance) Yamazaki et al., J Biol Chem 2003*
• IRef Biogrid Interaction: NRP1 — VEGFA (association, x-ray crystallography) Parker et al., J Biol Chem 2012*
• IRef Biogrid Interaction: NRP1 — VEGFA (direct interaction, pull down) Parker et al., J Biol Chem 2012*
• IRef Biogrid Interaction: NRP1 — VEGFA (direct interaction, pull down) Di Benedetto et al., Biochim Biophys Acta 2008*
• IRef Biogrid Interaction: NRP1 — VEGFA (direct interaction, pull down) Tirand et al., J Control Release 2006*
• IRef Biogrid Interaction: NRP1 — VEGFA (direct interaction, pull down) Allain et al., Cell Signal 2012*
• IRef Biogrid Interaction: NRP1 — VEGFA (direct interaction, pull down) Novoa et al., Bioorg Med Chem 2010*
• IRef Biogrid Interaction: NRP1 — VEGFA (direct interaction, pull down) Mamluk et al., J Biol Chem 2002
• IRef Biogrid Interaction: NRP1 — VEGFA (physical association, affinity chromatography technology) Soker et al., Cell 1998*
• IRef Biogrid Interaction: NRP1 — VEGFA (direct interaction, pull down) Soker et al., Cell 1998*
• MIPS CORUM NRP1-VEGFR2-VEGF(165) complex: NRP1-VEGFR2-VEGF(165) complex complex (KDR-NRP1-VEGFA) Pan et al., J Biol Chem 2007*
• MIPS CORUM VEGFA(165)-KDR-NRP1 complex: VEGFA(165)-KDR-NRP1 complex complex (KDR-NRP1-VEGFA) Soker et al., J Cell Biochem 2002*
• MIPS CORUM VEGFA(165)-VEGFR2-NRP1 complex: VEGFA(165)-VEGFR2-NRP1 complex complex (KDR-NRP1-VEGFA) Prahst et al., J Biol Chem 2008*
• MIPS CORUM NRP1-VEGF(165/121) complex: NRP1-VEGF(165/121) complex complex (NRP1-VEGFA) Pan et al., J Biol Chem 2007*
• IRef Corum Interaction: VEGFA — NRP1 (association, surface plasmon resonance) Pan et al., J Biol Chem 2007*
• IRef Corum Interaction: Complex of 13 proteins (association, anti bait coimmunoprecipitation) Prahst et al., J Biol Chem 2008*
• IRef Dip Interaction: VEGFA — NRP1 (direct interaction, cross-linking study) Tordjman et al., Blood 1999*
• IRef Dip Interaction: VEGFA — NRP1 (direct interaction, biochemical) Tordjman et al., Blood 1999*
• IRef Dip Interaction: VEGFA — NRP1 (direct interaction, cross-linking study) Migdal et al., J Biol Chem 1998*
• IRef Dip Interaction: VEGFA — NRP1 (direct interaction, coimmunoprecipitation) Whitaker et al., J Biol Chem 2001*
• IRef Hprd Interaction: NRP1 — VEGFA (in vivo) Makinen et al., J Biol Chem 1999*, Mamluk et al., J Biol Chem 2002, Shintani et al., EMBO J 2006*, Pan et al., Cancer Cell 2007*, Soker et al., Cell 1998*
• IRef Hprd Interaction: NRP1 — VEGFA (in vitro) Makinen et al., J Biol Chem 1999*, Mamluk et al., J Biol Chem 2002, Shintani et al., EMBO J 2006*, Pan et al., Cancer Cell 2007*, Soker et al., Cell 1998*
• IRef Intact Interaction: VEGFA — NRP1 (physical association, cross-linking study) Cecchi et al., Cancer Cell 2012*
• IRef Intact Interaction: VEGFA — NRP1 (physical association, cross-linking study) Shintani et al., EMBO J 2006*
• IRef Intact Interaction: VEGFA — NRP1 (physical association, anti tag coimmunoprecipitation) Shintani et al., EMBO J 2006*
• IRef Intact Interaction: VEGFA — NRP1 (physical association, anti bait coimmunoprecipitation) Shintani et al., EMBO J 2006*
• IRef Intact Interaction: VEGFA — NRP1 (physical association, enzyme linked immunosorbent assay) Pan et al., Cancer Cell 2007*
• IRef Ophid Interaction: VEGFA — NRP1 (aggregation, interologs mapping) Brown et al., Bioinformatics 2005
• IRef Ophid Interaction: VEGFA — NRP1 (aggregation, confirmational text mining) Soker et al., Cell 1998*

Text-mined interactions from Literome

Harper et al., J Cell Biochem 2001 : These cells did not express VEGFR-1 or VEGFR-2 so that VEGF binding to osteoblasts was strictly NRP1 dependent
Oh et al., Proc Natl Acad Sci U S A 2002 (Neovascularization, Pathologic) : Selective induction of neuropilin-1 by vascular endothelial growth factor ( VEGF ) : a mechanism contributing to VEGF induced angiogenesis
Deroanne et al., Oncogene 2002 : TSA inhibited in a dose dependent and reversible fashion the VEGF induced expression of VEGF receptors, VEGFR1, VEGFR2, and neuropilin-1
Bernatchez et al., J Cell Biochem 2002 : However, the role of NRP-1 in numerous VEGF-A activities remains unclear ... In contrast, stimulation of PAEC-Flt-1 and PAEC-NRP-1 with VEGF-A or VEGF-C did not induce proliferation, migration, or PAF synthesis ... In conclusion, the presence of NRP-1 on EC preferentially increases KDR activation by VEGF-A as well as KDR mediated biological activities, and may elicit novel intracellular events
Akagi et al., Br J Cancer 2003 (Stomach Neoplasms) : Neuropilin-1 (NRP-1) acts as a coreceptor for VEGF-165 and increases its affinity for VEGF receptor 2 (VEGFR-2) in endothelial cells
Watanabe et al., Am J Pathol 2004 (Anoxia...) : Dominant negative Ets-1 inhibited VEGF induced cell proliferation, tube formation, and the expression of neuropilin-1 and angiopoietin-2
Brusselmans et al., J Biol Chem 2005 (Anoxia) : Neuropilin-1 was involved in the VEGF-survival activity since overexpression of Nrp-1 decreased hypoxia induced apoptosis about 3-fold
Karihaloo et al., Mol Cell Biol 2005 : These morphogenic effects of VEGF-165 require activation of both VEGF receptor 2 (VEGFR-2) and neuropilin-1 (Nrp-1) , since neutralizing antibodies to either of these receptors or the addition of semaphorin 3A ( which blocks VEGF-165 binding to Nrp-1 ) prevents the morphogenic response and the phosphorylation of VEGFR-2 along with the downstream signaling
Mamluk et al., Angiogenesis 2005 : Previously, we have shown that the naturally occurring soluble form of NRP1 ( sNRP1 ) inhibits binding of VEGF ( 165 ) to endothelial cells in vitro and impairs tumor growth in vivo
Mac Gabhann et al., PLoS Comput Biol 2006 (Neoplasms) : Targeting neuropilin-1 to inhibit VEGF signaling in cancer : Comparison of therapeutic approaches
Hong et al., Clin Cancer Res 2007 (Carcinoma, Non-Small-Cell Lung...) : NRP1 and cancer cell invasion, angiogenesis, and signaling pathways were studied using NRP1 stimulation by vascular endothelial growth factor 165 ( VEGF ( 165 ) ) and NRP1 inhibition by small interfering RNAs ( siRNA ), soluble NRP1 ( sNRP1 ), and NRP1-inhibition peptides
Ji et al., Am J Physiol Heart Circ Physiol 2007 (Anoxia...) : We predict that expression of 10 ( 4 ) NRP1/cell can increase VEGF binding to receptors by 1.7-fold ( vs. no NRP1 ) ; in nonexercise trained muscle with PAD, angiogenesis is hindered due to limited VEGF upregulation, signaling, and gradients ; in exercise trained muscle, VEGF signaling is enhanced by upregulation of VEGFRs and NRP1 , and VEGF signaling is strongest within the first week of exercise therapy ; and hypoxia induced VEGF release is important to direct angiogenesis towards unperfused tissue
Banerjee et al., Biochemistry 2008 (Breast Neoplasms) : We found that VEGF-A 165 induces hAOSMC migration parallel with the induction of NRP-1 and VEGFR1 expressions and their associations along with the activation of PI3K/Akt
Zhang et al., Molecular cancer 2010 (Bone Neoplasms...) : Intriguingly, VEGF165 promoted physical interaction between NRP1 and hepatocyte growth factor (HGF) receptor c-MET, and facilitated c-MET phosphorylation via a NRP1 dependent mechanism
Genetos et al., Bone 2010 : This suggests that VEGF induction of Annexin A2 is not mediated via VEGF-R1 agonism alone but by VEGF-R1 and Neuropilin-1 or Neuropilin-2 heterodimers
Kim et al., Genes Dev 2011 : Therefore, although the Sema3E secreted by retinal neurons is evenly distributed throughout the retina, Sema3E-Plexin-D1 signaling is spatially controlled by VEGF through its regulation of Plexin-D1
Lee et al., Neoplasia (New York, N.Y.) 2013 (Breast Neoplasms...) : These studies demonstrate the antilymphangiogenic and antiangiogenic potential of the peptide against primary tumors and premetastatic, tumor conditioned regional LNs. Mechanistically, the peptide blocks vascular endothelial growth factor receptors 2 and 3 ( VEGFR2/3 ) and downstream proteins by binding to neuropilin 1/2 ( NRP1/2 ) and inhibiting VEGFR2/3 and NRP1/2 complex formation in the presence of VEGFA/C
Lanahan et al., Dev Cell 2013 (MAP Kinase Signaling System...) : Neuropilin 1 (NRP1) plays an important but ill defined role in VEGF-A signaling and vascular morphogenesis ... These results demonstrate that the NRP1 cytoplasmic domain promotes VEGFR2 trafficking in a PDZ dependent manner to regulate arteriogenic ERK signaling and establish a role for NRP1 in VEGF-A signaling during vascular morphogenesis
Soker et al., Cell 1998 : When coexpressed in cells with KDR, neuropilin-1 enhances the binding of VEGF165 to KDR and VEGF165 mediated chemotaxis