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Exon junction complex (EJC) activity is indispensable for Wg signaling by maintaining an appropriate level of Dsh (show DVL2 Proteins) protein for Wg ligand reception in Drosophila. Genetic and biochemical experiments demonstrate that Dlg1 protein acts independently from its role in cell polarity to protect Dsh (show DVL2 Proteins) protein from lysosomal degradation.
Banderuola (Bnd) is a novel regulator of asymmetric cell division (ACD (show ACD Proteins)). The data place Bnd at the top of the hierarchy of the factors involved in ACD (show ACD Proteins), suggesting that its main function is mediating localization and function of Dlg tumor suppressor.
The inactivation of cellular cortex polarization is the most likely target of dlg inactivation in mitosis.
Loss of scrib, dlg and lgl had no effect on gonad formation, but Dlg and Scrib in the gonadal mesoderm acted critically in the somatic wrapping of the pole cells and the internal structure of the Drosophila embryonic gonads.
Gliotactin and Discs large are co-regulated to maintain epithelial integrity.
Hts (show APCDD1 Proteins) regulates Dlg targeting to the neuromuscular junction in muscle and the lateral membrane of epithelial cells.
Electron microscopy reveals that during metamorphosis the subsynaptic reticulum vacuolizes in the early stages of synapse dismantling, concomitant with diffuse localization of Dlg.
DlgS97-Metro-DLin-7-type complexes control the proper organization of a synaptic junction; findings accentuate the importance of perisynaptic scaffold complexes for synaptic stabilization and organization
Study provide evidence that scrib and dlg function differentially in anterior and posterior patterning of the follicular epithelium at oogenesis. Further genetic analysis indicates that scrib and dlg act in a common pathway to regulate PFC (show CFP Proteins) fate induction.
integrins act through CaMKII activation to control the localization of dlg in the development of NMJ synaptic morphology
In Fmr1 (show FMR1 Proteins) KO neurons, Mdm2 (show MDM2 Proteins) is hyperphosphorylated, nuclear localized basally, and unaffected by MEF2 (show MEF2C Proteins) activation, which our data suggest due to an enhanced interaction with Eukaryotic Elongation Factor (show TSFM Proteins) 1alpha (EF1alpha), whose protein levels are elevated in Fmr1 (show FMR1 Proteins) KO. Expression of a dephosphomimetic of Mdm2 (show MDM2 Proteins) rescues PSD-95 ubiquitination, degradation and synapse elimination in Fmr1 (show FMR1 Proteins) KO neurons.
tested the effect of five targeted mouse mutations on the assembly of known PSD95 interactors, Kir2.3, Arc, IQsec2/BRAG1 and Adam22
Therefore, our study suggests that CREB and PSD95 are novel substrates of PERK, so inhibition of PERK phosphorylation using GSK2656157 would be beneficial against memory impairment after TBI.
PSD95 and SYP (show PTPN11 Proteins) may originate from the different sites, but they are closely related to the formation and maturation of synapse.
Expression levels of brain derived neurotrophic factor, postsynaptic density 95, and p-cyclic-AMP response element binding protein levels were significantly elevated in the testosterone (T) group, but flutamide reduced the T-induced effects in these biomarkers to control levels.
The results suggest that the neurological mechanisms of chronic stress on cognition might be associated with a decrease in hippocampal SYN (show SYP Proteins) and PSD95 expression, which is critical for structural synaptic plasticity.
critical roles of PSD-95 in regulating synaptic kainate receptors.
Phenylketonuric mice given a specific nutrient combination showed a significant reduction in PSD-95 expression in the hippocampus, specifically in the granular cell layer of the dentate gyrus, with a similar trend seen in the cornus ammonis 1 (CA1 (show CA1 Proteins)) and cornus ammonis 3 (CA3 (show CA3 Proteins)) pyramidal cell layer.
Lambda-cyhalothrin (LCT (show LCT Proteins)) could increase the PSD95 protein level via the ERalpha (show ESR1 Proteins)-dependent Akt (show AKT1 Proteins) pathway, and LCT (show LCT Proteins) might disrupt the up-regulation effect of estradiol on PSD95 protein expression via this signaling pathway.
Data indicate a contribution of D2 dopamine receptors to the effects of repetitive transcranial magnetic stimulation (rTMS) on postsynaptic density protein-95 (PSD-95) and cyclin-dependent kinase 5 (CDK5 (show CDK5 Proteins)) levels.
Phosphorylation at Y397 induced a significant increase in affinity for stargazing. The strategy presented here to generate site-specifically phosphorylated PDZ domains provides a detailed understanding of the role of phosphorylation in the regulation of PSD95 interactions.
This study demonstrated that a significant decrease in the protein level of PSD-95 in major depression disorder.
These results indicate that PKC (show PRRT2 Proteins) promotes synaptogenesis by activating PSD-95 phosphorylation directly through JNK1 (show MAPK8 Proteins) and calcium/calmodulin-dependent kinase II and also by inducing expression of PSD-95 and synaptophysin (show SYP Proteins).
The differences in cortical NMDAR (show GRIN1 Proteins) expression and post-synaptic density protein 95 are present in psychiatric disorders and suicide completion and may contribute to different responses to ketamine.
Mutation C>T at the rs13331 in the PSD95 gene is strikingly associated with an increased risk of autism spectrum disorders.
Data demonstrate a role for SNAP-25 (show SNAP25 Proteins) in controlling PSD-95 clustering and open the possibility that genetic reductions of the protein levels may contribute to the pathology through an effect on postsynaptic function and plasticity.
Data indicate the very high affinities of the trimeric ligands to postsynaptic density protein 95 (PSD-95) PDZ domains.
In this review, we focus on palmitoylation of PSD-95, which is a major postsynaptic scaffolding protein and makes discrete postsynaptic nanodomains in a palmitoylation-dependent manner and discuss a determinant role of local palmitoylation cycles
An association was found between reduced PSD95 in the prefrontal cortex and cognitive impairment in patients with either dementia with Lewy bodies or Parkinson's disease dementia.
Docosahexaenoic acid-containing phosphatidylcholines and PSD-95 decrease after loss of synaptophysin (show SYP Proteins) and before neuronal loss in patients with Alzheimer's disease.
This gene encodes a member of the membrane-associated guanylate kinase (MAGUK) family. It heteromultimerizes with another MAGUK protein, DLG2, and is recruited into NMDA receptor and potassium channel clusters. These two MAGUK proteins may interact at postsynaptic sites to form a multimeric scaffold for the clustering of receptors, ion channels, and associated signaling proteins. Multiple transcript variants encoding different isoforms have been found for this gene.
, disc large
, discs large
, disk large
, lethal(1)benign wing imaginal disc neoplasm
, lethal(1)discs large
, lethal(2)discs large
, discs, large homolog 4
, postsynaptic density protein 95
, disks large homolog 4
, PSD-95 alpha 2b
, PSD-95 beta
, discs large homolog 4
, synapse-associated protein 90
, synapse-associated protein SAP90
, Tax interaction protein 15
, post-synaptic density protein 95