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Gene Review

Dlg2  -  discs, large homolog 2 (Drosophila)

Mus musculus

Synonyms: A330103J02Rik, B230218P12Rik, B330007M19Rik, Channel-associated protein of synapse-110, Chapsyn-110, ...
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Disease relevance of Dlg2

  • Since platelet-activating factor is a potent neuronal injury mediator during the development of brain trauma, seizures, and ischemia, the present work suggests that PSD-93 might contribute to molecular mechanisms of neuronal damage in these brain disorders [1].

High impact information on Dlg2

  • Recombinant PSD-93 was phosphorylated by Fyn in vitro, and Tyr-384 was identified as a major phosphorylation site [2].
  • In addition, tyrosine-phosphorylated PSD-93 was able to bind to Csk, a negative regulator of Src family kinases, in vitro as well as in a brain lysate [2].
  • Identification of PSD-93 as a substrate for the Src family tyrosine kinase Fyn [2].
  • This suggests that PSD-93 might mediate many NMDA receptor-dependent physiological and pathophysiological functions [1].
  • These findings indicate that PSD-93 is involved in the NMDA receptor--nitric oxide-mediated pathological processing of neuronal damage triggered via platelet--activating factor receptor activation [1].

Biological context of Dlg2


Anatomical context of Dlg2

  • Chapsyn-110 mRNA was, though at low levels, found over the mantle zone of embryonic brains, and the level was progressively increased in the telencephalon starting at perinatal stages [4].
  • Furthermore, mice lacking PSD-93 exhibit blunted NMDAR-dependent persistent pain induced by peripheral nerve injury or injection of Complete Freund's Adjuvant, although they display intact nociceptive responsiveness to acute pain [5].
  • To assess the function of this protein complex at neuronal cholinergic synapses in vivo, we examined ganglia in mice that lack PSD93 [6].
  • METHODS: Postnatal day 7 wild-type (+/+), heterozygous (+/-), and homozygous (-/-) PSD-93 knockout mice were subjected to HI by permanent ligation of the right carotid artery, followed by exposure to 8% O2/92% N2 for 1 hour [3].

Associations of Dlg2 with chemical compounds


Co-localisations of Dlg2

  • We report here that PSD-93 colocalizes and interacts with the NMDA receptor and neuronal nitric oxide synthase in cultured cortical neurons [1].

Other interactions of Dlg2

  • Furthermore, GluRdelta2 and PSD-93 proteins were concentrated at the contacted portion of mismatched synapses, whereas AMPA receptors were distributed in both the contacted and dissociated portions [7].

Analytical, diagnostic and therapeutic context of Dlg2

  • After denervation, however, synaptic clusters of nAChRs disassemble much faster in mice lacking PSD93 than those in wild-type mice [6].


  1. Targeted disruption of PSD-93 gene reduces platelet-activating factor-induced neurotoxicity in cultured cortical neurons. Xu, Y., Zhang, B., Hua, Z., Johns, R.A., Bredt, D.S., Tao, Y.X. Exp. Neurol. (2004) [Pubmed]
  2. Identification of PSD-93 as a substrate for the Src family tyrosine kinase Fyn. Nada, S., Shima, T., Yanai, H., Husi, H., Grant, S.G., Okada, M., Akiyama, T. J. Biol. Chem. (2003) [Pubmed]
  3. Neonatal hypoxia-ischemia differentially upregulates MAGUKs and associated proteins in PSD-93-deficient mouse brain. Jiang, X., Mu, D., Sheldon, R.A., Glidden, D.V., Ferriero, D.M. Stroke (2003) [Pubmed]
  4. Distinct spatiotemporal expression of mRNAs for the PSD-95/SAP90 protein family in the mouse brain. Fukaya, M., Ueda, H., Yamauchi, K., Inoue, Y., Watanabe, M. Neurosci. Res. (1999) [Pubmed]
  5. Impaired NMDA receptor-mediated postsynaptic function and blunted NMDA receptor-dependent persistent pain in mice lacking postsynaptic density-93 protein. Tao, Y.X., Rumbaugh, G., Wang, G.D., Petralia, R.S., Zhao, C., Kauer, F.W., Tao, F., Zhuo, M., Wenthold, R.J., Raja, S.N., Huganir, R.L., Bredt, D.S., Johns, R.A. J. Neurosci. (2003) [Pubmed]
  6. PSD93 regulates synaptic stability at neuronal cholinergic synapses. Parker, M.J., Zhao, S., Bredt, D.S., Sanes, J.R., Feng, G. J. Neurosci. (2004) [Pubmed]
  7. Control of synaptic connection by glutamate receptor delta2 in the adult cerebellum. Takeuchi, T., Miyazaki, T., Watanabe, M., Mori, H., Sakimura, K., Mishina, M. J. Neurosci. (2005) [Pubmed]
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