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Gene Review

Dlg1  -  discs, large homolog 1 (Drosophila)

Mus musculus

Synonyms: B130052P05Rik, Disks large homolog 1, Dlgh1, E-dlg/SAP97, Embryo-dlg/synapse-associated protein 97, ...
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Disease relevance of Dlg1

  • Dlgh1(-/-) mice developed severe urinary tract abnormalities, including congenital hydronephrosis, which is the leading cause of renal failure in infants and children [1].
  • The importance of mLin-2/CASK in mammalian development is demonstrated by the fact that mutations in mLin-2/CASK or SAP97, another MAGUK protein, lead to cleft palate in mice [2].
  • BACKGROUND: The interaction of human T-cell leukemia virus type 1 (HTLV-1) Tax1 protein with the tumor suppressor Dlg1 is correlated with cellular transformation [3].

High impact information on Dlg1

  • Dlgh1 coordinates actin polymerization, synaptic T cell receptor and lipid raft aggregation, and effector function in T cells [4].
  • Using small interfering RNA and overexpression approaches, we show that Dlgh1 promotes antigen-induced actin polymerization, synaptic raft and TCR clustering, nuclear factor of activated T cell activity, and cytokine production [4].
  • We propose that Schwann cell-autonomous loss of Mtmr2-Dlg1 interaction dysregulates membrane homeostasis in the paranodal region, thereby producing outfolding and recurrent loops of myelin [5].
  • Dlg1 homologues have been located in several types of cellular junctions and play roles in cell polarity and membrane addition [5].
  • As such, SAP97 binding caused an intracellular accumulation of each Kv1 channel tested, through the accretion of SAP97 channel clusters in large (3-5 microm) ER-derived intracellular membrane vesicles [6].

Biological context of Dlg1

  • We propose that Dlgh1 coordinates TCR/CD28-induced actin-driven T cell synapse assembly, signal transduction, and effector function [4].
  • Dlgh1, a mouse homolog of the drosophila discs-large gene, is located on chromosome 16 [7].
  • Together, these results suggest that loss of Cx32 alters the levels, localization, and interactions of the tumor suppressor protein Dlgh1, events known in other systems to alter cell cycle and increase tumorigenicity [8].
  • Our data identify evolutionarily conserved protein-protein interaction domains that link mLin-2/CASK to SAP97 and account for their common phenotype when mutated in mice [2].
  • In agreement, coexpression of SAP97 and GluR1 in nonneuronal HEK293 cells increased both proteins compared with their single transfection, implying mutual stabilization [9].

Anatomical context of Dlg1


Associations of Dlg1 with chemical compounds


Other interactions of Dlg1


Analytical, diagnostic and therapeutic context of Dlg1

  • This translocation was confirmed by Western blots comparing Dlgh1 levels in nuclear extracts from wild type and Cx32 null murine livers [8].
  • Single-particle electron microscopy (EM) combined with biochemical measurements revealed the molecular shape of SAP97 and a monomer-dimer transition that depended on the N-terminal L27 domain [15].


  1. Discs-large homolog 1 regulates smooth muscle orientation in the mouse ureter. Mahoney, Z.X., Sammut, B., Xavier, R.J., Cunningham, J., Go, G., Brim, K.L., Stappenbeck, T.S., Miner, J.H., Swat, W. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  2. A novel and conserved protein-protein interaction domain of mammalian Lin-2/CASK binds and recruits SAP97 to the lateral surface of epithelia. Lee, S., Fan, S., Makarova, O., Straight, S., Margolis, B. Mol. Cell. Biol. (2002) [Pubmed]
  3. Inactivation of tumor suppressor Dlg1 augments transformation of a T-cell line induced by human T-cell leukemia virus type 1 Tax protein. Ishioka, K., Higuchi, M., Takahashi, M., Yoshida, S., Oie, M., Tanaka, Y., Takahashi, S., Xie, L., Green, P.L., Fujii, M. Retrovirology (2006) [Pubmed]
  4. Dlgh1 coordinates actin polymerization, synaptic T cell receptor and lipid raft aggregation, and effector function in T cells. Round, J.L., Tomassian, T., Zhang, M., Patel, V., Schoenberger, S.P., Miceli, M.C. J. Exp. Med. (2005) [Pubmed]
  5. Disruption of Mtmr2 produces CMT4B1-like neuropathy with myelin outfolding and impaired spermatogenesis. Bolino, A., Bolis, A., Previtali, S.C., Dina, G., Bussini, S., Dati, G., Amadio, S., Del Carro, U., Mruk, D.D., Feltri, M.L., Cheng, C.Y., Quattrini, A., Wrabetz, L. J. Cell Biol. (2004) [Pubmed]
  6. PSD-95 and SAP97 exhibit distinct mechanisms for regulating K(+) channel surface expression and clustering. Tiffany, A.M., Manganas, L.N., Kim, E., Hsueh, Y.P., Sheng, M., Trimmer, J.S. J. Cell Biol. (2000) [Pubmed]
  7. Dlgh1, a mouse homolog of the drosophila discs-large gene, is located on chromosome 16. Burgess, D.L., Rafael, J.A., Meisler, M.H., Chamberlain, J.S. Mamm. Genome (1996) [Pubmed]
  8. The gap junction protein connexin32 interacts with the SRC homology 3/hook domain of discs large homolog 1. Duffy, H.S., Iacobas, I., Hotchkiss, K., Hirst-Jensen, B.J., Bosco, A., Dandachi, N., Dermietzel, R., Sorgen, P.L., Spray, D.C. J. Biol. Chem. (2007) [Pubmed]
  9. Brain-derived neurotrophic factor signal enhances and maintains the expression of AMPA receptor-associated PDZ proteins in developing cortical neurons. Jourdi, H., Iwakura, Y., Narisawa-Saito, M., Ibaraki, K., Xiong, H., Watanabe, M., Hayashi, Y., Takei, N., Nawa, H. Dev. Biol. (2003) [Pubmed]
  10. Craniofacial dysmorphogenesis including cleft palate in mice with an insertional mutation in the discs large gene. Caruana, G., Bernstein, A. Mol. Cell. Biol. (2001) [Pubmed]
  11. Synaptic glutamate receptor clustering in mice lacking the SH3 and GK domains of SAP97. Klöcker, N., Bunn, R.C., Schnell, E., Caruana, G., Bernstein, A., Nicoll, R.A., Bredt, D.S. Eur. J. Neurosci. (2002) [Pubmed]
  12. The cytoplasmic domain of NrCAM binds to PDZ domains of synapse-associated proteins SAP90/PSD95 and SAP97. Dirks, P., Thomas, U., Montag, D. Eur. J. Neurosci. (2006) [Pubmed]
  13. Microtubule-associated protein light chain 2 is a stargazin-AMPA receptor complex-interacting protein in vivo. Ives, J.H., Fung, S., Tiwari, P., Payne, H.L., Thompson, C.L. J. Biol. Chem. (2004) [Pubmed]
  14. Structural characterization of the intermolecular interactions of synapse-associated protein-97 with the NR2B subunit of N-methyl-D-aspartate receptors. Wang, L., Piserchio, A., Mierke, D.F. J. Biol. Chem. (2005) [Pubmed]
  15. Quaternary structure, protein dynamics, and synaptic function of SAP97 controlled by L27 domain interactions. Nakagawa, T., Futai, K., Lashuel, H.A., Lo, I., Okamoto, K., Walz, T., Hayashi, Y., Sheng, M. Neuron (2004) [Pubmed]
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