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Gene Review

DLG2  -  discs, large homolog 2 (Drosophila)

Homo sapiens

Synonyms: Channel-associated protein of synapse-110, Chapsyn-110, Disks large homolog 2, PPP1R58, PSD-93, ...
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Disease relevance of DLG2


High impact information on DLG2

  • In this issue of Neuron, Elias et al. have elucidated the roles of three MAGUKs, PSD-95, PSD-93, and SAP-102, in the targeting of AMPA receptors to synapses in hippocampal neurons [3].
  • At immature synapses, PSD-95 and PSD-93 play little role in synaptic AMPA-R clustering; instead, SAP-102 dominates [4].
  • Chapsyn-110 associates tightly with the postsynaptic density in brain, and mediates the clustering of both NMDA receptors and K+ channels in heterologous cells [5].
  • In the ultrastructural studies that are described here, PSD-93 localizes to both postsynaptic densities and dendritic microtubules of cerebellar Purkinje neurons [6].
  • PSD-93 is expressed in discrete neuronal populations as well as in specific non-neuronal cells, and it exhibits complex molecular diversity attributable to tissue-specific alternative splicing [7].

Biological context of DLG2

  • Yeast two-hybrid screening of a human brain cDNA library using the carboxyl terminus of Kir2.1 as bait yielded cDNA encoding the first two PDZ domains of PSD-93, but with an extended N-terminal region that diverged from other PSD-93 isoforms [8].
  • RESULTS: We have identified new isoform of DLG2 gene, which contains 3'-end exons of the known DLG2 gene along with the hypothetical gene FLJ37266 [2].
  • In addition, PSD-93 clusters delta2 when they are coexpressed in heterologous cells, and clustering is disrupted by point mutations of delta2 that disrupt the delta2-PSD-93 interaction [9].

Anatomical context of DLG2


Associations of DLG2 with chemical compounds


Other interactions of DLG2

  • We introduced a double mutation (I38A/I40A) into the N-terminal domain of hDlg, which disrupted its interaction with DLG2, a key event in the membrane targeting of hDlg [11].
  • We found significant changes in the expression of NF-L in DLPFC, and PSD-95 and PSD-93 in ACC; increased transcript expression was associated with decreased protein expression, suggesting abnormal translation and/or accelerated protein degradation of these molecules in schizophrenia [12].
  • One of these proteins, PSD-93, co-localizes with a subpopulation of nNOS in the macula densa [13].
  • PSD-93 and beta-catenin are also enriched at alpha3-nAChR postsynaptic sites [14].


  1. Fetal life in Down syndrome starts with normal neuronal density but impaired dendritic spines and synaptosomal structure. Weitzdoerfer, R., Dierssen, M., Fountoulakis, M., Lubec, G. J. Neural Transm. Suppl. (2001) [Pubmed]
  2. Differential expression of a new isoform of DLG2 in renal oncocytoma. Zubakov, D., Stupar, Z., Kovacs, G. BMC Cancer (2006) [Pubmed]
  3. Promiscuous Interactions between AMPA-Rs and MAGUKs. Fitzjohn, S.M., Doherty, A.J., Collingridge, G.L. Neuron (2006) [Pubmed]
  4. Synapse-Specific and Developmentally Regulated Targeting of AMPA Receptors by a Family of MAGUK Scaffolding Proteins. Elias, G.M., Funke, L., Stein, V., Grant, S.G., Bredt, D.S., Nicoll, R.A. Neuron (2006) [Pubmed]
  5. Heteromultimerization and NMDA receptor-clustering activity of Chapsyn-110, a member of the PSD-95 family of proteins. Kim, E., Cho, K.O., Rothschild, A., Sheng, M. Neuron (1996) [Pubmed]
  6. Localization of postsynaptic density-93 to dendritic microtubules and interaction with microtubule-associated protein 1A. Brenman, J.E., Topinka, J.R., Cooper, E.C., McGee, A.W., Rosen, J., Milroy, T., Ralston, H.J., Bredt, D.S. J. Neurosci. (1998) [Pubmed]
  7. Cloning and characterization of postsynaptic density 93, a nitric oxide synthase interacting protein. Brenman, J.E., Christopherson, K.S., Craven, S.E., McGee, A.W., Bredt, D.S. J. Neurosci. (1996) [Pubmed]
  8. An alternatively spliced isoform of PSD-93/chapsyn 110 binds to the inwardly rectifying potassium channel, Kir2.1. Leyland, M.L., Dart, C. J. Biol. Chem. (2004) [Pubmed]
  9. Postsynaptic density-93 interacts with the delta2 glutamate receptor subunit at parallel fiber synapses. Roche, K.W., Ly, C.D., Petralia, R.S., Wang, Y.X., McGee, A.W., Bredt, D.S., Wenthold, R.J. J. Neurosci. (1999) [Pubmed]
  10. SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit. Leonard, A.S., Davare, M.A., Horne, M.C., Garner, C.C., Hell, J.W. J. Biol. Chem. (1998) [Pubmed]
  11. Protein 4.1-mediated membrane targeting of human discs large in epithelial cells. Hanada, T., Takeuchi, A., Sondarva, G., Chishti, A.H. J. Biol. Chem. (2003) [Pubmed]
  12. Changes in NMDA receptor subunits and interacting PSD proteins in dorsolateral prefrontal and anterior cingulate cortex indicate abnormal regional expression in schizophrenia. Kristiansen, L.V., Beneyto, M., Haroutunian, V., Meador-Woodruff, J.H. Mol. Psychiatry (2006) [Pubmed]
  13. Protein-protein interactions controlling nitric oxide synthases. Kone, B.C. Acta Physiol. Scand. (2000) [Pubmed]
  14. Neuronal nicotinic synapse assembly requires the adenomatous polyposis coli tumor suppressor protein. Temburni, M.K., Rosenberg, M.M., Pathak, N., McConnell, R., Jacob, M.H. J. Neurosci. (2004) [Pubmed]
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