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DLG3 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. Additionally we are shipping DLG3 Antibodies (104) and DLG3 Proteins (6) and many more products for this protein.
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This family broadens the mutational and phenotypical spectrum of DLG3-associated non-syndromic X-linked intellectual disability and demonstrates that heterozygous female mutation carriers can be as severely affected as males.
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 ELISA Kits) and PLC (show HSPG2 ELISA Kits)-beta3 mutually regulate each other is far more complex than a simple, two-state allosteric model and instead is probably kinetically determined.
Following the critical period NMDA receptor function was unaffected by loss of SAP102 but there was a reduction in the divergence of TC connectivity. These data suggest that changes in synaptic function early in development caused by mutations in SAP102 result in changes in network connectivity later in life.
Insertion of a guanine into the DLG3 5' UTR (show UTS2R ELISA Kits), 7 bp upstream of the start codon, down regulated DLG3 protein levels. This non-coding variant segregates with X-linked intellectual disability in a large family.
We propose that unliganded PLC (show HSPG2 ELISA Kits)-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 ELISA Kits)-beta modulates Gbetagamma access to its binding site.
the MCP1 (show CCL2 ELISA Kits)-induced cortactin (show CTTN ELISA Kits) phosphorylation is dependent on PLCb3 (show PLCB3 ELISA Kits)-mediated PKC activation, and siRNA-mediated down-regulation of either of these molecules prevents cortactin (show CTTN ELISA Kits) interaction with WAVE2 (show WASF2 ELISA Kits)
Gnb isoforms control a signaling pathway comprising Rac1, Plcbeta2, and Plcbeta3 leading to LFA-1 (show ITGAL ELISA Kits) activation and neutrophil arrest in vivo
Trans-homophilic interaction of CADM1 (show CADM1 ELISA Kits) activates PI3K (show PIK3CA ELISA Kits) by forming a complex with MAGuK-family proteins MPP3 (show MPP3 ELISA Kits) and Dlg (show DLG4 ELISA Kits).
miR (show MLXIP ELISA Kits)-1246 might play a role in neurological pathogenesis of human enterovirus 71 by regulating DLG3 gene in infected cells.
our current study identified a functional interplay between PSD-95 (show DLG4 ELISA Kits) and synapse-associated protein 102 (SAP102) to regulate synaptic AMPA (show GRIA3 ELISA Kits) receptors
SAP102 has a fundamental role in trafficking the NMDA receptor complex to the synaptic sites.
The Dlg3 have functions in complex cognitive processes.
Synapse associated protein 102 (SAP102) binds the C-terminal part of the scaffolding protein neurobeachin (show NBEA ELISA Kits).
Dlg3 exerts a distinct function by recruiting the ubiquitin ligases Nedd4 and Nedd4-2 through its PPxY motifs. These interactions are required for Dlg3 monoubiquitination, apical membrane recruitment, and tight junction consolidation.
Membrane-associated guanylate kinase (show GUK1 ELISA Kits) homolog SAP102 is a central organizers of the postsynaptic density at excitatory synapses on pyramidal neurons.
SAP102 interacts with the PDZ-binding domain of Sec8, a member of the exocyst complex. nteractions between the two proteins are involved in the delivery of N-methyl-D-aspartate receptors to the cell surface in heterologous cells and neurons.
SAP102 was required for normal spatial learning. Loss of SAP102 results in changes in spatial strategy usage. Altered long term potentiation and spike-timing-dependent plasticity in SAP102 mutants. Couples NMDA receptors to MAPK/ERK (show MAPK1 ELISA Kits) pathway.
Results describe E-dlg (show DLG4 ELISA Kits), a mouse homologue of the Drosophila discs large (show DLG4 ELISA Kits) tumor suppressor (Dlg (show DLG4 ELISA Kits), also known as SAP97), that binds preferentially to SAP102.
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.
disks large homolog 3
, synapse-associated protein 102
, 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3
, PLC beta 3
, phosphoinositide phospholipase C-beta-3
, discs large homolog 3
, discs, large homolog 3 (neuroendocrine-dlg, Drosophila)
, membrane protein, palmitoylated 3 (MAGUK p55 subfamily member 3)
, PSD-95/SAP90-related protein 1