How do cells finely tune the activity of phosphoinositide-specific phospholipase C? This review explores the regulation of phosphoinositide-specific phospholipase C (PLC), focusing on the eleven distinct isoforms identified in mammals. These isoforms, grouped into four subfamilies (β, γ, δ, and ∍), catalyze the hydrolysis of phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2] to inositol 1,4,5-trisphosphate and diacylglycerol upon activation of cell surface receptors. Each PLC isoform possesses X and Y domains forming the catalytic core, along with regulatory domains common to signaling proteins. These domains target PLC isozymes to their substrate or activators through protein-protein or protein-lipid interactions. The review also explores the distinct regulatory domains in PLC isoforms renders them susceptible to different modes of activation. Ultimately, the intricate regulation of PLC isoforms highlights the complex mechanisms through which cellular signaling pathways are modulated. Given that the partners that interact with these regulatory domains of PLC isozymes are generated or eliminated in specific regions of the cell in response to changes in receptor status, the activation and deactivation of each PLC isoform are likely highly regulated processes.
Published in the Annual Review of Biochemistry, this paper aligns perfectly with the journal's focus on providing comprehensive and up-to-date overviews of key biochemical processes. By detailing the regulation of PLC isoforms and their diverse activation mechanisms, the review contributes valuable insights to biochemists studying cell signaling pathways, maintaining the journal's reputation for high-impact content.
| Category | Category Repetition |
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