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Data suggest that 300-residue C-terminal domain of PLCB3 promotes adsorption to phospholipid monolayer/membrane bilayer and is required for spatial organization/adsorption of PLCB3 on membrane surface; defects in phosphatidylinositol 4,5-bisphosphate (PIP2) hydrolysis alter monolayer adsorption, thus, suggesting role of active site in this process; PLCB3 is preferentially adsorbed to region of bilayer enriched with PIP2.
These results indicate that the mechanism by which Galphaq (show GNAQ Proteins) and PLC (show HSPG2 Proteins)-beta3 mutually regulate each other is far more complex than a simple, two-state allosteric model and instead is probably kinetically determined.
We propose that unliganded PLC (show HSPG2 Proteins)-beta exists in equilibrium between a closed conformation observed in crystal structures and an open conformation where the PH domain moves away from the EF hands. Therefore, intrinsic movement of the PH domain in PLC (show HSPG2 Proteins)-beta modulates Gbetagamma access to its binding site.
the MCP1 (show CCL2 Proteins)-induced cortactin (show CTTN Proteins) phosphorylation is dependent on PLCb3-mediated PKC (show PRRT2 Proteins) activation, and siRNA-mediated down-regulation of either of these molecules prevents cortactin (show CTTN Proteins) interaction with WAVE2 (show WASF2 Proteins)
Gnb isoforms control a signaling pathway comprising Rac1, Plcbeta2, and Plcbeta3 leading to LFA-1 (show ITGAL Proteins) activation and neutrophil arrest in vivo
membranes are integral for the activation of PLC (show HSPG2 Proteins)-beta isozymes by diverse modulators.
the M3 muscarinic receptor (show CHRM3 Proteins) maximizes the efficiency of PLCbeta3 signaling beyond its canonical role as a guanine nucleotide exchange factor (show RASGRF1 Proteins) for Galpha (show SUCLG1 Proteins).
This study provides an understanding of the structural basis for the PDZ-mediated NHERF1 (show SLC9A3R1 Proteins)-PLCbeta3 interaction that could prove valuable in selective drug design against CXCR2 (show CXCR2 Proteins)-related cancers.
PLCbeta3 is enriched in the cytosol.
phospholipase C (show PLC Proteins)-beta3 structure reveals the role of the its distal C-terminal domain
Schmerle (she) encodes a zebrafish ortholog of Phospholipase C, beta 3 (Plcbeta3) which is required in cranial neural crest cells for Edn1 regulation of pharyngeal arch patterning.
investigation of physiological involvement of PLCbeta3 signaling in ovulatory-size follicles: identification of PLCbeta3 as a mediator of LH-induced differentiation responses of granulosa cells; up-regulation of PLCbeta3 during oogenesis/ovulation
Data, including data from studies using transgenic/knockout mice, suggest that Ppp1ca (show PPP1CA Proteins) and Gnb1 (show GNB1 Proteins) interact in quiescent platelets; then, Ppp1ca (show PPP1CA Proteins) and Plcb3 interact during platelet aggregation; thus, Gnb1 (show GNB1 Proteins) enlists Ppp1ca (show PPP1CA Proteins) to modulate G protein-coupled receptor (show GPR34 Proteins) signaling. (Ppp1ca (show PPP1CA Proteins) = protein phosphatase 1 (show PPP1CB Proteins), catalytic subunit alpha; Gnb1 (show GNB1 Proteins) = guanine nucleotide-binding protein (show TRIM23 Proteins), subunit beta-1; Plcb3 = phospholipase C (show PLC Proteins), subunit beta-3)
Plcb3-deficient mice spontaneously develop atopic dermatitis-like skin lesions.
Data suggest that PLCbeta3 acts as a negative regulator of VEGF- (vascular endothelial growth factor A (show VEGFA Proteins)-) mediated vascular hyperpermeability through intracellular calcium signaling.
GPCR (show GPBAR1 Proteins) activation of Ras and PI3Kc in neutrophils depends on PLCb2 (show PLCb2 Proteins)/b3 and the RasGEF RasGRP4 (show RASGRP4 Proteins).
defined a PLC-beta3- and SHP-1-mediated signaling pathway for FcvarepsilonRI-mediated cytokine production
Cellular G(i)-G(q) synergism derives from direct supra-additive stimulation of phospholipase C (show PLC Proteins)-beta3 by G protein subunits Gbetagamma and Galpha(q (show GNAQ Proteins)).
Expression of Plcb3 was studied in a cell line during myoblast differentiation.
both PLCbeta2/beta3 and PI3Kgamma (show PIK3CG Proteins) play vital roles in platelet cytoskeletal dynamics
results suggest that activation of PLC (show HSPG2 Proteins)-b3 by pertussis toxin-sensitive G proteins is responsible for transient [Ca2 (show CA2 Proteins)+]i increase in response to thrombin (show F2 Proteins)
This gene encodes a member of the phosphoinositide phospholipase C beta enzyme family that catalyze the production of the secondary messengers diacylglycerol and inositol 1,4,5-triphosphate from phosphatidylinositol in G-protein-linked receptor-mediated signal transduction. Alternative splicing results in multiple transcript variants.
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3
, PLC beta 3
, phosphoinositide phospholipase C-beta-3
, 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3
, phospholipase C beta 3
, phospholipase C-beta-3
, phospholipase C, beta 3 (phosphatidylinositol-specific)
, 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3-like