1. Transactivation of PDGFRβ by dopamine D4receptor does not require PDGFRβ dimerization.
- Author
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Sum Shing Chi, Vetiska, Sandra M., Gill, Robin S., Hsiung, Marilyn S., Fang Liu, and Van Tol, Hubert H. M.
- Subjects
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PHOSPHORYLATION , *CHEMICAL reactions , *PROTEIN-tyrosine kinases , *G proteins , *MEMBRANE proteins , *AMINO acids , *NEUROTRANSMITTER receptors , *DOPAMINE receptors , *PLATELET-derived growth factor - Abstract
Growth factor-induced receptor dimerization and cross-phosphorylation are hallmarks of signal transduction via receptor tyrosine kinases (RTKs). G protein-coupled receptors (GPCRs) can activate RTKs through a process known as transactivation. The prototypical model of RTK transactivation involves ligand-mediated RTK dimerization and cross-phosphorylation. Here, we show that the platelet-derived growth factor receptor β (PDGFRβ) transactivation by the dopamine receptor D4 (DRD4) is not dependent on ligands for PDGFRβ. Furthermore, when PDGFRβ dimerization is inhibited and receptor phosphorylation is suppressed to near basal levels, the receptor maintains its ability to be transactivated and is still effective in signaling to ERK1/2. Hence, the DRD4-PDGFRβ-ERK1/2 pathway can occur independently of a PDGF-like ligand, PDGFRβ cross-phosphorylation and dimerization, which is distinct from other known forms of transactivation of RTKs by GPCRs. [ABSTRACT FROM AUTHOR]
- Published
- 2010
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