{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPhospholipase C‐β3 (PLCB3) is a key effector enzyme in G protein–coupled receptor (GPCR) signaling that directly engages activated G proteins. High‐resolution structural studies have shown that PLCB3 binds activated Gαq through a conserved module and employs an extended C-terminal domain to promote precise membrane targeting and optimal orientation for lipid hydrolysis. In addition, biochemical analyses reveal that PLCB3 is subject to autoinhibition via a structural “plug” that is released upon membrane anchoring, thereby facilitating a rapid “catch‐and‐release” mode of G protein engagement. Moreover, the pleckstrin homology (PH) domain of PLCB3 mediates binding to Gβγ subunits, and its propensity to form homodimers – further modulated by interactions with regulatory proteins such as calmodulin – adds an additional layer of control over enzyme activity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFunctionally, PLCB3 is indispensable across a range of cellular contexts. At the trans-Golgi network, its production of diacylglycerol (DAG) triggers the activation of kinases such as PKCη and PKD, which are critical for the fission of transport carriers. In innate immune cells – including neutrophils, macrophages, and T lymphocytes – PLCB3 contributes to synergistic inositol triphosphate generation and calcium release, thereby potentiating Ras-dependent pathways, integrin activation, and chemotactic responses. In endothelial and vascular smooth muscle cells, PLCB3 signaling governs actin remodeling, migration, and proliferation through cross talk with receptor tyrosine kinases and GPCRs. In addition, phosphorylation of PLCB3, particularly at serine 1105, plays a central role in integrating signals from oxytocin, cAMP/PKA, and PKC pathways in myometrial and glomerular mesangial cells, while in airway epithelial cells, PLCB3 supports CFTR-dependent chloride secretion and the activation of calcium-dependent chloride channels."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional layers of regulation are provided by PLCB3’s participation in multiprotein complexes. For instance, binding of PDZ domain–containing proteins such as PDZK1 to the C-terminal PDZ ligand of PLCB3 fosters the formation of a ternary complex with somatostatin receptors, thereby amplifying receptor-stimulated inositol phosphate production and calcium signaling. Likewise, interactions with the oxysterol-binding protein ORP4L facilitate the translocation of PLCB3 from nuclear stores to the plasma membrane through a mechanism involving RAN activation and VAPA association. Collectively, these protein–protein interactions – in concert with regulatory events such as covalent modifications, dynamic dimerization, and conformational changes within critical domains – ensure that PLCB3 precisely modulates second messenger production and fine-tunes downstream signaling events. This multifaceted regulation underscores the enzyme’s integral roles in normal cellular function and its potential impact on pathophysiological processes, including cancer, cystic fibrosis, and inflammatory disorders."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "20", "end_ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Gary L Waldo, Tiffany K Ricks, Stephanie N Hicks, et al. 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