Phospho-PDGFR beta (Y751) Recombinant Rabbit Monoclonal Antibody [PSH13-61]

Function

Platelet Derived Growth Factor (PDGF) is a mitogen for mesenchyme- and glia-derived cells. PDGF consists of two chains, A and B, which dimerize to form functionally distinct isoforms, PDGF-AA, PDGF-AB, and PDGF-BB. These three isoforms bind with different affinities to two receptor types, a and b, which are endowed with protein tyrosine kinase domains and undergo either homo- or heterodimerization as a consequence of ligand binding. Ligand stimulation of PDGFR-b leads to autophosphorylation at Tyr-857, which is the major autophosphorylation site, and Tyr-751, which is the major in vitro phosphorylation site. Autophosphorylation of Tyr-751, which lies in the kinase insert region, is required for binding of phosphatidylinositol-3 kinase to the receptor. These auto-phosphorylation events largely contribute to signal transduction through the PDGF receptor. Mutations in PDGFRB are mainly associated with the clonal eosinophilia class of malignancies.

Background References

1. Kumar, A. et al. 2010. Platelet-derived growth factor-DD targeting arrests pathological angiogenesis by modulating glycogen synthase kinase-3beta phosphorylation. J. Biol. Chem. 285: 15500-15510.

2. Siegbahn, A. et al. 2008. TF/FVIIa transactivate PDGFRbeta to regulate PDGF-BB-induced chemotaxis in different cell types: involvement of Src and PLC. Arterioscler. Thromb. Vasc. Biol. 28: 135-141.

Subcellular Location

Cell membrane, Cytoplasmic vesicle, Lysosome lumen.

UNIPROT

SwissProt: P09619 Human

SwissProt: P05622 Mouse

SwissProt: Q05030 Rat

Synonyms