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• W2116566070 abstract "The functional activity of Cdc42 is known to be regulated by proteins that control its GDP/GTP-bound state. However, there is still limited information on how Cdc42 is controlled by G-protein-coupled receptors. Adenosine receptors belong to the G-protein-coupled receptor family of cell surface receptors. Human HMC-1 mast cells express the high-affinity A_2A and the low-affinity A_2B subtypes of adenosine receptors known to increase intracellular cAMP levels. We found that both subtypes of A₂ adenosine receptors activate Cdc42 in HMC-1 cells. Furthermore, stimulation of adenylate cyclase with forskolin, or loading of HMC-1 with the cell-permeable cAMP analog 8-Br-cAMP, activated Cdc42. Stimulation of Cdc42 by cAMP was also observed in CHO-K1 and COS-7 cells. Protein kinase A (PKA)-mediated phosphorylation is likely involved in cAMP-dependent Cdc42 activation, because transient expression of the PKA catalytic subunit in COS-7 cells activated Cdc42. Inhibition of protein phosphatases 1 and 2A with calyculin A potentiated the effects of 5′-<i>N</i>-ethylcarboxamidoadenosine and 8-Br-cAMP, whereas the selective PKA inhibitor H-89 reversed the activation of Cdc42. We demonstrated that Cdc42 is a poor substrate for PKA phosphorylation in vitro and in intact cells. Our data suggest that PKA does not phosphorylate Cdc42 directly. Instead, the proteins that modulate the GDP/GTP-bound state of Cdc42 may be the primary targets of PKA phosphorylation." @default.
• W2116566070 created "2016-06-24" @default.
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• W2116566070 date "2000-11-01" @default.
• W2116566070 modified "2023-10-15" @default.
• W2116566070 title "Cyclic AMP and Protein Kinase A Stimulate Cdc42: Role of A₂Adenosine Receptors in Human Mast Cells" @default.
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• W2116566070 doi "https://doi.org/10.1124/mol.58.5.903" @default.
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