Phorbol diesters promote β-adrenergic receptor phosphorylation and adenylate cyclase desensitization in duck erythrocytes
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A novel molecular mechanism involved in the crosstalks between homologous and PKC-mediated heterologous regulatory pathway of dopamine D<inf>2</inf> receptor
2020, Biochemical PharmacologyCitation Excerpt :Heterologous regulation occurs at low agonist concentration and affects the stimulated receptors as well as other inactive receptors on the same cell. Second messenger-dependent protein kinases, such as protein kinase A and C (PKC), mediate heterologous regulation by phosphorylating the receptors in the cytoplasmic regions regardless of agonist occupancy [8,51]. Even though two regulatory processes occur via different mechanisms, there have been reports showing the mutual interactions between PKC and GRK2/β-arrestins.
β-Arrestin2 directly or through GRK2 inhibits PKCβII activation in a ubiquitination-dependent manner
2018, Biochimica et Biophysica Acta - Molecular Cell ResearchCitation Excerpt :Conversely, heterologous GPCR regulation is mediated by second messengers, which are mostly produced via the activation of adjacent receptors. Second messenger-dependent protein kinases, such as protein kinase A (PKA), and C (PKC), mediate heterologous GPCR regulation by heterologously phosphorylating both agonist occupied, and unoccupied GPCRs [6,7]. Maintaining normal interactions between the homologous and heterologous pathways is critical to ensure the correct regulation of GPCR functions.
A phosphodiesterase inhibitor, cilomilast, enhances cAMP activity to restore conditioned odor preference memory after serotonergic depletion in the neonate rat
2009, Neurobiology of Learning and MemoryAltered β-adrenoceptor function associated to protein kinase C activation in hyperproliferative T lymphocytes
2000, Journal of NeuroimmunologyGravin-mediated formation of signaling complexes in β<inf>2</inf>-adrenergic receptor desensitization and resensitization
2000, Journal of Biological ChemistryCitation Excerpt :Protein kinase C has been shown to modulate the function of several G-protein-linked receptors, and consensus sites for phosphorylation have been identified in many of these receptors. Although a few early studies suggested that activation of protein kinase C desensitizes the β2-adrenergic receptors (38, 39), most subsequent studies reported either no effect of protein kinase C activation on desensitization (40, 41) or frank potentiation of β2-adrenergic receptor signaling rather than desensitization (42-48). Protein kinase C is associated in complex with the receptor-gravin complex in unstimulated cells.