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The human homologue of the Drosophila discs large tumor suppressor protein (hDlg) is a member of the MAGUKs (membrane associated guanylate kinases) protein family. Members of this family (PSD-95, ZO-1, ZO-2, and human erythroid p55) are involved in cell structure and signaling events. The hDlg protein consists of several domains: three PDZ (PSD-95/Discs large/ZO-1) domains, an SH3 domain, and a guanylate kinase-like domain. However, hDlg contains a proline rich N-terminus region consisting of two SH3 domain binding sites that are not normally found in the MAGUKs family. The PDZ domains mediate the interaction of several proteins, such as Shaker-type K channel proteins and the APC tumor suppressor protein. Dlg is a peripheral membrane that associates with the cytoskeleton. The cellular location and binding sites of Dlg suggest a role in structure, signal transduction, and growth regulation. Supporting these probable Dlg functions are reports demonstrating that recessive mutations in Drosophila dlg lead to imaginal disc neoplasia and death. Also, Dlg has been reported to bind p56 [lck] tyrosine kinase and the Kv1.3 channel in human T lymphocytes.
