Angiogenesis, the formation of new blood vessels from pre-existing vasculature, is central to a number of physiological conditions, from embryogenesis to wound healing in adults and is a hallmark of pathological conditions such as tumorigenesis [1-3]. Angiogenesis is mediated by the coordinated action of a variety of growth factors, metabolites and cell adhesion molecules in endothelial cells [4-6]. Vascular endothelial growth factor (VEGF) is the principal angiogenic growth factor modulating neovascularization [7]. The biological effect of VEGF is mediated through specific VEGF receptors on endothelial cell surface. VEGFs (VEGF-A, VEGF-B, VEGF-C and VEGF-D) interact with VEGF receptors such as VEGFR1, VEGFR2 and VEGFR3. Among them, VEGFA/VEGFR2 signaling appears to mediate cellular responses involved in angiogenesis prominently. Further, VEGF/VEGFR1 signaling, though weak, converges to VEGFR2 signaling pathway. VEGFA binding to VEGFR2 at the surface of endothelial cells leads to dimerization and auto-phosphorylation of specific tyrosine residues in the cytoplasmic domain of VEGFR2. It leads to activation of multiple downstream signaling cascades and promotes endothelial cell proliferation, migration, and tube formation relevant to angiogenesis [8]. VEGFR2 dependent activation of PI3K-AKT-mTOR signaling regulates cell survival, cell proliferation, anti-apoptotic and cell permeability functions [9]. Another important pathway of VEGF mediated cell proliferation appears to be through PLCγ-mediated activation of PKC and downstream induction of the ERK and other PKC-dependent pathways [10]. Endothelial cell migration is induced by VEGFA/VEGFR2 signaling through activation of p38MAPK (actin polymerization) and FAK (focal adhesion turnover) which is particularly important in directed migration. Phosphosite specificity towards downstream signalling has also been documented. Phosphosite mapping documented seven phosphosites in VEGFR2 receptor: Y1054, Y1214, Y801, Y1175, Y951, Y1059 and Y996. Phosphorylation of Y1214 and Y1054 regulates signaling events involved in cell migration. Y801 phosphorylation regulates cell survival. Y1175 regulates both cell proliferation and migration. Y951 and Y1059 phosphorylation regulates cell survival, cell migration and cell proliferation. VEGFA/VEGFR2 signaling network compiles data available in the literature with respect to VEGFA signaling (especially VEGFA-165) through VEGFR2 in endothelial cells. The signaling events involving these proteins were derived from experimentally validated data involving multiple experimental techniques and approaches. Individual signaling events in VEGFR2 signaling networks leading to cell proliferation, migration and survival were identified and categorized into protein-protein interactions, enzyme-catalyzed events, activation/inhibition reactions, transport of protein across subcellular compartments, and gene regulation events. Signaling molecules involved in VEGFA/VEGFR2 signaling were categorized to enzymes, receptors and transcription factors and the contextual activation/deactivation of these molecules downstream to VEGFA/ VEGFR2 signaling, in modulating angiogenesis, is documented. VEGFA dependent angiogenesis pathway map depicts the integration of signaling pathways regulating cell survival, cell migration, cell proliferation, cellular interactions downstream of VEGFA/VEGFR2 signaling relevant to angiogenesis, regulation of VEGFR2, phosphosite specificity of VEGFR2 towards downstream signaling, post-translational modifications, molecular function-based information, cross-talks among proteins in the canonical signaling modules and the information on the compartmentalization of proteins. The map of VEGFA/VEGFR2 signaling network is interactive to help investigators to add new information as it becomes available in the future for analysis or representation. VEGFA dependent angiogenesis pathway map may please be cited as: 1. Abhinand, C. S., Raju, R., Soumya, S. J., Arya, P. S., and Sudhakaran, P. R. (2016). VEGF-A/VEGFR2 signaling network in endothelial cells relevant to angiogenesis. Journal of cell communication and signaling, 10(4), 347-354. 2. 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Nat Rev Mol Cell Biol. e4c cdf d5a f61 eec f61 e6d bcb e4c cdf b44 b44 b44 b44 c70 bae aa4 d77 b63 fcc cd2 d77 b7b e05 f3d dda b4d b2d bfb b10 b10 e73 c51 a15 a15 c51 e73 f51 b32 c3e ac1 bfb ee5 fc8 a13 bff d35 fb0 d0d aa6 af4 f51 c74 da7 df9 caa a13 db7 dc7 de8 b90 a03 e05 The extracellular domain of EGFR interacts with EGF to form a receptor complex structure containing EGF.EGFR complex in a 2:2 stoichiometry. e55 ab6 f73 bfb d5d bf0 e55 b08 fd2 db3 dfb a57 dfb dfb e20 dfb dfb e55 b5b c13 b5b b31 b31 b31 b31 e55 db8 d0f caa caa caa caa bae a51 a51 c64 a51 e55 b90 d5d d5d d5d dcd bb1 c2e c2e a07 c2e c2e b3f c71 c71 dd5 eab eab eab eab eab eab a57 ef1 a57 a57 a57 eea eea eea f23 f69 b63 b63 b15 ad7 b15 ad7 b15 b37 adf f4d eed e4c df9 ed0 df9 df9 df9 f73 df9 fe9 db8 fe9 Ubiquitination fe9 fe9 eea df9 f30 f30 d35 d0d eea f2e ac1 f2e ac1 b08 ac1 d35 bff d35 d6b ae7 ab6 d0f d0f d0f a2d a2d a2d a2d a2d da3 e05 ad4 a4e a4e a4e ad4 ffc bcb bcb a4d a4d fc6 bef bef bef a4d b0c b0c Dephosphorylation ccc f0a f0a f0a f0a c18 c18 c18 c18 a8b a8b a8b f4c f48 a8b a8b c74 a8b a2d e0b a8b ff2 ff2 ff2 a22 e7e eca ff2 e19 e19 e19 f10 db5 f10 f4c f10 f61 f23 f10 e20 e20 e20 d6b adf adf a2e a25 a25 b56 a25 b86 b86 b86 b58 af4 c37 af4 af4 f51 f51 efd db8 db8 a2e a4e a03 d5f a13 b58 Dephosphorylation e0b e26 Dephosphorylation e0b e26 Dephosphorylation e0b b32 b32 b32 b32 dde bf0 dde bf0 bf0 ad4 ad4 ad4 b2d b2d b2d b4d b2d b2d ba5 a8b Dephosphorylation ab1 Dephosphorylation ab1 f44 b0c d93 bb1 d93 b7d b7d b7d b70 bd4 b9c b3d bd4 cef bd4 b9c b3d d21 b70 d61 b70 e66 b70 d61 bb1 a01 a01 a01 a01 c3e c3e c64 bfb bfb bfb c96 f77 efd f4c bfb e41 bfb ee5 ee5 ee5 ee5 e41 db5 e41 e41 e41 e41 e41 e41 e41 e41 e55 b58 f69 f23 f23 f23 a72 f4b f4b f4b a72 b2d ff6 ff6 a62 a62 e10 e10 cc8 cc8 cc8 cc8 cc8 e10 ea3 ea3 e94 Dephosphorylation e94 c43 Dephosphorylation fcc e5c e5c e5c eaf eaf df3 df3 adf df3 df3 adf e4c df3 df3 df3 df3 df3 df3 df3 df3 b8f b8f b8f b8f b8f b8f b8f a4e a4e a4e ad4 a4e ad4 a4e f33 a62 d3d d3d d3d da7 da7 da7 d0f a0f a0f a8e a8e f89 d99 bb6 d77 de0 bb6 ecc d7e d77 d6f d6f de0 b22 ec7 cb6 d7e cae cb6 d7e cae cb6 d7e cae d7e d21 bff d35 d99 bb6 d77 de0 b22 ec7 b22 f71 b21 b22 c4d a99 f71 d99 bd6 f71 bd6 f09 eca eca e7e c13 c13 c74 c74 c74 c74 c74 ed2 ed2 Ubiquitination fc5 Ubiquitination fc5 b49 e09 Ubiquitination fc5 Ubiquitination fc5 Ubiquitination fc5 b56 b56 c03 c03 d23 b56 df9 c03 d23 b56 c03 d23 b56 bd6 c03 d23 b56 bd6 d0d d0d e35 Ubiquitination fc5 de8 The extracellular domain of EGFR interacts with EGF to form a receptor complex structure containing EGF.EGFR complex in a 2:2 stoichiometry. f43 c87 c87 f43 eaa d12 f43 fc8 fc8 fc8 d3f fc8 f51 c51 d0f ab0 bff d35 fb0 fb0 https://www.webmedcentral.com/wmcpdf/Article_WMC001111.pdf c1d https://www.webmedcentral.com/wmcpdf/Article_WMC001111.pdf c1d cef bd4 cef Y951 Y1214 Ubiquitination Dephosphorylation e02 f3c a1b d1f f58 b50 a46 f04 a27 e89 d59 d71 d71 d71 d71 f3b f19 d79 b13 b13 Y1214 db3 The extracellular domain of EGFR interacts with EGF to form a receptor complex structure containing EGF.EGFR complex in a 2:2 stoichiometry. db1 db1 db1 ab6 ab6 bcb a4e bcb a4e bcb ad7 b15 b37 adf f4d f8b f8b b79 a28 dbc f50 dbc bed ca4 b48 c52 c52 c1b c1b b29 b29 b29 c4a b33 ae0 fb5 d31 d31 d31 http://www.oapublishinglondon.com/article/471 a27 3494473, 8639530, 2783412, 3257758, 1988447, 1856216, 19531499 3494473, 8639530, 2783412, 3257758, 1988447, 1856216, 19531499 3494473, 8639530, 2783412, 3257758, 1988447, 1856216, 19531499 c9d 20422004 PubMed Extracellular SOD-derived H2O2 promotes VEGF signaling in caveolae/lipid rafts and post-ischemic angiogenesis in mice. 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