Reactome | VEGF ligand-receptor interactions

VEGF ligand-receptor interactions

Stable Identifier

R-HSA-194313

DOI

10.3180/REACT_12380.1

Type

Pathway

Species

Homo sapiens

Compartment

plasma membrane

ReviewStatus

5/5

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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
16336962	Signal transduction by VEGF receptors in regulation of angiogenesis and lymphangiogenesis Shibuya, M, Claesson-Welsh, L	Exp Cell Res	2006
16633338	VEGF receptor signalling - in control of vascular function Dimberg, A, Kreuger, J, Olsson, AK, Claesson-Welsh, L	Nat Rev Mol Cell Biol	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 Matsumoto, T, Cross, MJ, Dixelius, J, Claesson-Welsh, L	Trends Biochem Sci	2003