VEGF ligand-receptor interactions

Stable Identifier
R-HSA-194313
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Pathway
Species
Homo sapiens
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The VEGF family is encoded by seven genes (VEGF-A, B, C, D, E: PLGF (Placenta Growth Factor)-1, 2). Six isoforms of VEGF-A protein, containing 121, 145, 165, 183, 189, and 206 amino acid residues, and two isoforms of VEGF-B (167 and 186 residues) are specified by alternatively spliced mRNAs. The active form of each of these proteins is a homodimer.
The specificities of the three VEGF tyrosine kinase receptors, VEGFR-1, VEGFR-2 and VEGFR-3, for these ligands are shown in the figure (Hicklin and Ellis 2005). All VEGF-A isoforms bind both VEGFR-1 and VEGFR-2; PLGF-1 and -2, and VEGF-B isoforms bind only VEGFR-1; VEGF-E binds VEGFR-2; and VEGF-C and -D bind both VEGFR-2 and -3. VEGF-D undergoes a complex series of post-translational modifications that results in secreted forms with increased activity toward VEGFR-3 and VEGFR-2.
Two co-receptor proteins in the cell membrane, neuropilin (NRP)-1 and NRP-2, interact with VEGFR proteins to increase the affinity of the latter for their ligands (Neufeld et al.,2002). They differ from VEGFR proteins in not having intracellular signaling domains.

Literature References
PubMed ID Title Journal Year
16633338 VEGF receptor signalling - in control of vascular function

Olsson, AK, Dimberg, A, Kreuger, J, Claesson-Welsh, L

Nat Rev Mol Cell Biol 2006
16336962 Signal transduction by VEGF receptors in regulation of angiogenesis and lymphangiogenesis

Shibuya, M, Claesson-Welsh, L

Exp Cell Res 2006
16835467 Signal transduction via vascular endothelial growth factor (VEGF) receptors and their roles in atherogenesis

Matsumoto, T, Mugishima, H

J Atheroscler Thromb 2006
13678960 VEGF-receptor signal transduction

Cross, MJ, Dixelius, J, Matsumoto, T, Claesson-Welsh, L

Trends Biochem Sci 2003
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