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• W2495682007 abstract "This chapter focuses on effector enzymes adenylyl cyclase and phosphoilipase C (PLC) and their regulation. Adenylyl cyclases catalyze the formation of cyclic AMP (cAMP), a second messenger in metabolic regulation. The presence of nutrients signals the activation of adenylyl cyclase through the RAS proteins. In starvation conditions, the ratio of GTP- to GDP-bound RAS declines, as a result, the cellular content of cAMP declines, growth ceases and the cells switch to meiosis and spore formation. A number of proteins and other agents can activate or inhibit adenylyl cyclase: the known physiological activators and inhibitors include the subunits of the heterotrimeric G- proteins and Ca2+. The chapter describes the structural organization and regulation of adenylyl cyclases by GTP-binding proteins, Ca2+, phosphorylation, aluminum floride, forskolin, and cholera and pertussis toxins. Inositol-containing phospholipids, such as phosphatidylinositol-4,5-bisphosphate (PI-4,5-P2) and inositol-l,4,5-triphosphate (IP3) have role in cell regulation. These phospholoipids require the activation of a plasma membrane-associated enzyme of the phospholipase C (PLC) family. A number of PLC isoforms have been purified and cloned, that fall into three main classes: β, γ, and δ. There are two ways in which PLC may be activated to hydrolyse PI(4,5)P2. One of these involves G-proteins and the other a protein tyrosine kinase." @default.
• W2495682007 created "2016-08-23" @default.
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• W2495682007 date "2002-01-01" @default.
• W2495682007 modified "2023-10-18" @default.
• W2495682007 title "Effector enzymes coupled to GTP-binding proteins" @default.
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• W2495682007 doi "https://doi.org/10.1016/b978-012289631-6/50025-9" @default.
• W2495682007 hasPublicationYear "2002" @default.
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