VEGFA-VEGFR2 signaling (WP3888)

Homo sapiens

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. Sunitha, P., Raju, R., Sajil, C.K., Abhinand, C.S., Nair, A.S., Oommen, O.V., Sugunan, V.S., and Sudhakaran, P.R. (2019). Temporal VEGFA responsive genes in HUVECs: Gene signatures and potential ligands/receptors fine-tuning angiogenesis. Journal of Cell Communication and Signaling, 13, 561 - 571. References [1] Folkman J (1971). Tumor angiogenesis: therapeutic implications. N Engl J Med. 285:1182-1186. [2] Chatterjee S, Heukamp LC, Siobal M et al., 2013. Tumor VEGF: VEGFR2 autocrine feed-forward loop triggers angiogenesis in lung cancer. J Clin Invest. 123:1732-1740. [3] Shibuya M (2014). VEGF-VEGFR Signals in Health and Disease. BiomolTher (Seoul). 22:1-9. [4] Kumar VB, Binu S, Soumya SJ et al., 2014. Regulation of vascular endothelial growth factor by metabolic context of the cell. Glycoconj J. 31:427-434. [5] Kitazume S, Imamaki R, Ogawa K et al., 2014. Sweet role of platelet endothelial cell adhesion molecule in understanding angiogenesis. Glycobiology. 24:1260-1264. [6] Kunhiraman H, Edatt L, Thekkeveedu S et al., 2016. 2‐Deoxy Glucose Modulates Expression and Biological Activity of VEGF in a SIRT‐1 Dependent Mechanism. J Cell Biochem. [7] Lohela M, Bry M, Tammela T et al., 2009. VEGFs and receptors involved in angiogenesis versus lymphangiogenesis. Curr Opin Cell Biol. 21:154-165. [8] Koch S, Claesson-Welsh L, 2012. Signal transduction by vascular endothelial growth factor receptors. Cold Spring Harbor perspectives in medicine. 2(7):a006502. [9] Koch S, Tugues S, Li X et al., 2011. Signal transduction by vascular endothelial growth factor receptors. Biochem J.437:169-183. [10] Simons M, Gordon E, Claesson-Welsh L. 2016. Mechanisms and regulation of endothelial VEGF receptor signalling. Nat Rev Mol Cell Biol.


Dr.P.R.Sudhakaran , Kristina Hanspers , Alex Pico , Egon Willighagen , Denise Slenter , and Eric Weitz


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Homo sapiens




Pathway Ontology

vascular endothelial growth factor signaling pathway

Cell Type Ontology

endothelial cell


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FGD5 Protein ncbigene:152273
LMO2 Protein ncbigene:405
TAL1 Protein ncbigene:6886
GATA2 Protein ncbigene:2624
LDB2 Protein ncbigene:9079
DLL4 Protein ncbigene:54567
GPX1 Protein ncbigene:2876
GJA1 Protein ncbigene:2697
CYCS Protein ncbigene:54205
MAP2K3 Protein ncbigene:5606
CHAC1 Protein ncbigene:79094
C15ORF39 Protein ncbigene:56905
RAB37 Protein ncbigene:326624
ADRB2 Protein ncbigene:154
TRAF3IP2 Protein ncbigene:10758
DUSP5 Protein ncbigene:1847
EPHA2 Protein ncbigene:1969
FJX1 Protein ncbigene:24147
TMEM170A Protein ncbigene:124491
SDF2L1 Protein ncbigene:23753
SLC2A14 Protein ncbigene:144195
IER5 Protein ncbigene:51278
SLC39A14 Protein ncbigene:21356
ZNF555 Protein ncbigene:148254
HLX Protein ncbigene:3142
NRARP Protein ncbigene:441478
SLC25A25 Protein ncbigene:114789
CCRL2 Protein ncbigene:9034
PNP Protein ncbigene:4860
APOLD1 Protein ncbigene:81575
PIK3R1 Protein ncbigene:5295
NDRG1 Protein ncbigene:10397
FUT1 Protein ncbigene:2523
DLL4 Protein ncbigene:54567
SIAH2 Protein ncbigene:6478
CASC10 Protein ncbigene:399726
TRPC3 Protein ncbigene:7222
SLC7A1 Protein ncbigene:6541
BRD4 Protein ncbigene:23476
LARP7 Protein ncbigene:51574
CREBBP Protein ncbigene:1387
MEF2C Protein ncbigene:4208
CXCL8 Protein ncbigene:3576
BMP2 Protein ncbigene:650
SEMA6D Protein ncbigene:80031
NR4A2 Protein ncbigene:4929
ADAMTS9 Protein ncbigene:56999
EGR3 Protein ncbigene:1960
NR4A1 Protein ncbigene:3164
IGFBP3 Protein ncbigene:3486
CYBB Protein ncbigene:1536
NOX4 Protein ncbigene:50507
EPHB2 Protein ncbigene:2048
SDCBP Protein ncbigene:6386
ABL1 Protein ncbigene:25
RCAN1 Protein ncbigene:1827
TNFRSF25 Protein ncbigene:8718
PTPN6 Protein ncbigene:5777


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