Recombinant Rat Disks large homolog 1 (Dlg1), partial

1. Results indicate that the GluA1 subunit accessory protein SAP97 may represent a novel target for pharmacotherapeutic intervention in the treatment of cocaine craving PMID: 26149358
2. dendrite branching promoting action of full length SAP97 depends on ligand(s) that bind to the PDZ3 domain. PMID: 25701814
3. The data establish a prominent role for PDZ2 and I3 domains of SAP97 in organizing the ss1-adrenergic receptosome involved in connecting the ss1-AR to trafficking and signaling networks. PMID: 23696820
4. Acute BDNF treatment upregulates the interactions between AMPA receptor subunits (GluR1 and GluR2) with their scaffold proteins SAP97 and GRIP1, respectively. PMID: 23460828
5. studies show that SAP97 interactions with CRFR1 attenuate CRFR1 endocytosis and that SAP97 is involved in coupling G protein-coupled receptors to the activation of the ERK1/2 signaling pathway. PMID: 23576434
6. Scribble/Lgl/Dlg polarity protein complex is a regulator of blood-testis barrier dynamics and spermatid polarity during spermatogenesis PMID: 23038739
7. Cx32 is differentially phosphorylated and exists in a complex with SAP97 and CaM. PMID: 22718765
8. Overexpression of SAP97 was associated with overexpression of PSD-95 and recruitment of nNOS to the synapse and was accompanied by marked morphological changes, with spines enwrapping and engulfing presynaptic terminals. PMID: 20865734
9. SAP97 isoforms can regulate the ability of synapses to undergo plasticity by controlling the surface distribution of AMPA and NMDA receptors. PMID: 21768261
10. investigation of structure of SAP97 isoforms: Data suggest conformation of SAP97 is determined by nature of N-terminus, which may, in turn, influence specific role of a particular splice variant. (signal sequence involved in mitochondrial targeting) PMID: 22242544
11. SAP97 and dystrophin macromolecular complexes determine two pools of cardiac sodium channels Nav1.5 in cardiomyocytes. PMID: 21164104
12. Upregulation of SAP97 coincides with the redistribution of aquaporin (AQP)4 and inwardly-rectifying potassium channel (Kir) 4.1 in blue light-injured rat retina. PMID: 20625331
13. In cardiac myocytes SAP97 regulates surface expression of channels underlying I(K1) PMID: 20530486
14. Following acute injection of phencyclidine SAP-97 transcripts are upregulated in the adult neocortex. PMID: 19836928
15. findings show that, in Schwann cells, Dlg1 interacts with PTEN to inhibit axonal stimulation of myelination; this mechanism limits myelin sheath thickness & prevents overmyelination in sciatic nerves PMID: 20448149
16. CaMKIIalpha targets a specific SAP97 splice variant to disengage AKAP79/150 from regulating GluR1 AMPARs PMID: 19858198
17. As monitored by circular dichroism and differential scanning calorimetry, SAP97 (T(m)=64 degrees C) is significantly more thermal stable than SAP90/PSD-95 (T(m)=52 degrees C) and follows a bimodal phase transition. PMID: 19632332
18. Binding to GluR-A AMPA receptor subunit is determined by a novel sequence motif PMID: 12070168
19. findings suggest that synapse associated protein 97/NR2A NMDA receptor interaction is regulated by calcium calmodulin dependent protein kinase II-dependent phosphorylation PMID: 12933808
20. a complex composed of SAP97, CASK, Veli, and Mint1 associates with Kir2 channels via the C-terminal PDZ-binding motif. SAP97, Veli-1, or Veli-3 binds directly to the Kir2.2 C terminus and recruits CASK PMID: 14960569
21. in T cells, Discs large (Dlg1) is recruited upon activation to cortical actin and forms complexes with early participants in T cell activation PMID: 15263016
22. data highlight the potential role of abnormalities in the subcellular distribution of Synapse-associated proteins PSD-95 and SAP97 in the pathophysiology of a neurological disease PMID: 15703272
23. a direct interaction between SAP97 and PSD-95 may play a functional role in the trafficking and clustering of AMPA receptors. PMID: 16332687
24. These results suggest that SAP97 may play a central role in the coordinated growth of synapses during development and plasticity by recruiting a complex of postsynaptic proteins that enhances presynaptic terminal growth. PMID: 16495462
25. Profound modifications of NR2B subunit association with synapse-associated protein-97 occurs in 6-OHDA, L-DOPA -treated dyskinesia. PMID: 16540568
26. Interaction between synthetic GluR-A C-terminal peptides and the PDZ2 domain of SAP97. Last 4 residues of GluR-A peptides bind to PDZ2 in a fashion typical of class I PDZ interactions. PMID: 16634638
27. These results demonstrate that the different N termini of the predominant endogenous forms of PSD-95 (alpha-isoform) and SAP97 (beta-isoform) govern their role in regulating synaptic function. PMID: 16815335
28. SAP97 was expressed postsynaptically at the climbing fibers synapse at early ages during Purkinje cell dendritic growth; its expression changed from neurons to Bergmann glia once these glial cells had completed their enwrapping process. PMID: 17335044
29. calcium/calmodulin-dependent protein kinase II (CaMKII)-dependent SAP97 phosphorylation regulates the subcellular localization of Kv4.2. PMID: 17635915
30. We speculate that restricted dynamics & preferential Kir2.1 binding to PDZ2 are features that enable SAP97 to function as a scaffold protein, allowing other proteins to bind to other 2 PDZ domains in sufficient proximity to yield productive channelosomes. PMID: 18004877
31. The distribution of SAP97 confirms that this protein is actually an integral component of the PSD, and suggests that it may have a role in inserting or stabilizing its main binding partner, Glu-R1, at the edge of the PSD. PMID: 18392731
32. SAP97 is a major partner for surface expression and CaMKII-dependent regulation of cardiac Kv4.2 and kv4.3 channels. PMID: 19213956
33. N-terminal splicing of SAP97 controls synaptic strength by regulating distribution of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors. PMID: 19357261
34. Our data demonstrate that the retention and trafficking of NMDARs in this endoplasmic reticulum subcompartment requires both CASK and SAP97. PMID: 19620977
35. SAP97 regulates Kir2.3 channels by multiple mechanisms. PMID: 19633205

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KEGG: rno:25252

STRING: 10116.ENSRNOP00000055672

UniGene: Rn.89331