Activation and inhibition of erythropoietin receptor function: role of receptor dimerization.

G-protein Coupled Receptor Dimerization

A growing body of evidence suggests that GPCRs exist and function as dimers or higher oligomers. The evidence for GPCR dimerization comes from biochemical, biophysical and functional studies. In addition, researchers have shown the occurrence of heterodimerization between different members of the GPCR family. Two receptors can interact with each other to make a dimer through their extracellular...

Structure, function, and activation of the erythropoietin receptor.

RYTHROPOIETIN (EPO) is the principal growth factor E that promotes the viability, proliferation, and differentiation of mammalian erythroid progenitor cells, functions that are transduced by the specific cell surface EPO receptor (EPO-R). In contrast to many other hematopoietic growth factors, EPO primarily affects relatively mature erythroid cells, although it may also influence the growth and...

Ligand-Induced, Receptor-Mediated Dimerization and Activation of EGF Receptor

The EGF receptor mediates many cellular responses in normal biological processes and in pathological states. Recent structural studies reveal the molecular basis for ligand binding specificity and how ligand binding induces receptor dimerization. Receptor dimerization is mediated by receptor-receptor interactions in which a loop protruding from neighboring receptors mediates receptor dimerizati...

Mechanism of FGF receptor dimerization and activation

Fibroblast growth factors (fgfs) are widely believed to activate their receptors by mediating receptor dimerization. Here we show, however, that the FGF receptors form dimers in the absence of ligand, and that these unliganded dimers are phosphorylated. We further show that ligand binding triggers structural changes in the FGFR dimers, which increase FGFR phosphorylation. The observed effects d...

Development of Radiolabeled Recombinant Erythropoietin for Receptor Studies