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A homozygous loss of function variant in PLCB3 is associated with corneal dystrophy, developmental delay and spondylometaphyseal dysplasia.
These results, besides identifying S845L as a loss-of-function variant, strengthen the importance of targeting PLCB3 to mitigate the cystic fibrosis inflammatory response in bronchial epithelial cells without blunting the immune response.
This study reveals detailed mechanistic insight into the role of ORP4L in PLCbeta3 redistribution from storage within the nucleus to the plasma membrane via RAN activation and interaction with VAPA in Jurkat T-cells.
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 and PLC-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-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-beta modulates Gbetagamma access to its binding site.
the MCP1-induced cortactin phosphorylation is dependent on PLCb3-mediated PKC activation, and siRNA-mediated down-regulation of either of these molecules prevents cortactin interaction with WAVE2
Gnb isoforms control a signaling pathway comprising Rac1, Plcbeta2, and Plcbeta3 leading to LFA-1 activation and neutrophil arrest in vivo
membranes are integral for the activation of PLC-beta isozymes by diverse modulators.
the M3 muscarinic receptor maximizes the efficiency of PLCbeta3 signaling beyond its canonical role as a guanine nucleotide exchange factor for Galpha.
This study provides an understanding of the structural basis for the PDZ-mediated NHERF1-PLCbeta3 interaction that could prove valuable in selective drug design against CXCR2-related cancers.
PLCbeta3 is enriched in the cytosol.
phospholipase C-beta3 structure reveals the role of the its distal C-terminal domain
GPCR activation of Ras and PI3Kc in neutrophils depends on PLCb2/b3 and the RasGEF RasGRP4.
PDZ domain-containing 1 (PDZK1) protein regulates phospholipase C-beta3 (PLC-beta3)-specific activation of somatostatin by forming a ternary complex with PLC-beta3 and somatostatin receptors.
Stromal cell-derived factor-1 signaling via the CXCR4-TCR heterodimer uses PLC-beta3 to activate the Ras-ERK pathway and increase intracellular calcium ion concentrations
Data demonstrate that PLCB3, by regulating intracellular calcium transients, plays a relevant role in amplifying the expression and release of IL-8, the major chemokine recruiting neutrophils in CF airway lungs.
Activation of hPLCbeta3 by U73122 required covalent modification of cysteines as evidenced by the observation that enzyme activation was attenuated by thiol-containing nucleophiles, l-cysteine and glutathione.
Studies indicate that the complex between the effector protein phospholipase C-beta3 (PLC-beta3) and its activator, Galpha(q), suggests that several effectors independently evolved a structurally similar helix-turn-helix segment for G protein recognition.
study describe the structure of PLC-beta3 in an activated complex with Galphaq, which together with supporting biochemical and physiological analyses reveals its mechanism of transmembrane signaling
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 and Gnb1 interact in quiescent platelets; then, Ppp1ca and Plcb3 interact during platelet aggregation; thus, Gnb1 enlists Ppp1ca to modulate G protein-coupled receptor signaling. (Ppp1ca = protein phosphatase 1, catalytic subunit alpha; Gnb1 = guanine nucleotide-binding protein, subunit beta-1; Plcb3 = phospholipase C, 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-) mediated vascular hyperpermeability through intracellular calcium signaling.
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-beta3 by G protein subunits Gbetagamma and Galpha(q).
Expression of Plcb3 was studied in a cell line during myoblast differentiation.
both PLCbeta2/beta3 and PI3Kgamma play vital roles in platelet cytoskeletal dynamics
results suggest that activation of PLC-b3 by pertussis toxin-sensitive G proteins is responsible for transient [Ca2+]i increase in response to thrombin
GPCR agonists ET-1, LPA, and thrombin activate PLCepsilon and PLCbeta3 in fibroblasts. Activation of these PLC isoforms displays agonist-specific temporal profiles; PLCbeta3 is predominantly involved in acute and PLCepsilon in sustained PI hydrolysis
The pattern of phospholipase Cbeta3 expression is unique, revealing stripes in three of the four transverse zones and a uniform distribution in the fourth. and PLCbeta3 is restricted to the zebrin II-immunopositive Purkinje cell subset.
These results demonstrate that PLCbeta3 is required to mediate "itch" sensation in response to histamine acting on the histamine H1 receptor in C-fiber nociceptive neurons.
PLCbeta3 plays a major role in mediating mGluR1-dependent synaptic transmission, plasticity, and integration in PLCbeta3-dominant Purkinje cells
loss of PLCbeta2 and PLCbeta3 significantly impaired T cell migration.
a novel role for PLC activity in promoting macrophage survival in atherosclerotic plaques and identify PLC beta3 as a potential target for treatment of atherosclerosis.
PLCbeta3 may provide a selective target for inhibiting Ca(2+) responses to mediators of inflammation, including C5a, UDP, PAF, and LPA
Deficiencies in PLC-beta3 are associated with the development of myeloproliferative disease, lymphoma, and other tumors.
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