anti-Discs, Large Homolog 3 (Drosophila) (DLG3) Anticorps

Human Discs, Large Homolog 3 (Drosophila) (DLG3) interaction partners

1. These data provide evidence for a novel mechanism in regulating SAP102 function and glutamate receptor trafficking.

2. 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.

3. 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.

4. Insertion of a guanine into the DLG3 5' UTR, 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.

5. Trans-homophilic interaction of CADM1 activates PI3K by forming a complex with MAGuK-family proteins MPP3 and Dlg.

6. miR-1246 might play a role in neurological pathogenesis of human enterovirus 71 by regulating DLG3 gene in infected cells.

7. These data shed new light on the role of SAP102 in the regulation of NMDAR trafficking.

8. This study identified DLG3 significantly associated loci with a biologically plausible role in schizophrenia.

9. The data of this study suggested that DLG3 is down-regulated in this cancer type.

10. The PDZ-independent interaction between SAP102 and GluN2B mediates the synaptic clearance of GluN2B-containing NMDARs.(SAP102 protein)

11. Synapse associated protein 102 (SAP102) binds the C-terminal part of the scaffolding protein neurobeachin.

12. A total of six novel and 11 known single nucleotide polymorphisms were identified. Further studies are warranted to analyze the candidate genes at Xq11.1-q21.33.

13. DLG3 was identified by genome-wide gene expression analyses as correlated with cellular sensitivity to cisplatin and carboplatin. DLG3 was also found to correlate with cellular sensitivity to platinating agents in NCI-60 cancer cell lines.

14. DLG3 did not associate with non-syndromic mental retardation in Chinese Han population; however, further studies are needed.

15. Results identified a novel splice site mutation in the disc-large homolog 3 (DLG3) gene, encoding the synapse-associated protein 102 (SAP102) in one out of 300 families with moderate to severe non-syndromic mental retardation.

16. Loss may lead to altered synaptic plasticity and may explain the intellectual impairment observed in individuals with DLG3 mutations

17. E6AP is extensively involved in the ubiquitin-mediated degradation of Dlg (an HPV E6-dependent substrate) as a cellular E3 ubiquitin-protein ligase.

18. The results of this study suggested a putative role for DLG3/SAP102 in cortical hyperexcitability and epileptogenicity of malformations of cortical development.

Mouse (Murine) Discs, Large Homolog 3 (Drosophila) (DLG3) interaction partners

1. 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.

2. our current study identified a functional interplay between PSD-95 and synapse-associated protein 102 (SAP102) to regulate synaptic AMPA receptors

3. SAP102 has a fundamental role in trafficking the NMDA receptor complex to the synaptic sites.

4. The Dlg3 have functions in complex cognitive processes.

5. Synapse associated protein 102 (SAP102) binds the C-terminal part of the scaffolding protein neurobeachin.

6. 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.

7. Membrane-associated guanylate kinase homolog SAP102 is a central organizers of the postsynaptic density at excitatory synapses on pyramidal neurons.

8. 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.

9. 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 pathway.

10. Results describe E-dlg, a mouse homologue of the Drosophila discs large tumor suppressor (Dlg, also known as SAP97), that binds preferentially to SAP102.

11. SAP102 and PSD-95 regulate the synaptic trafficking of distinct glutamate receptor subtypes at different developmental stages, thereby playing necessary roles in excitatory synapse development.