Discs Large, Drosophila, Homolog Of, 1 OKDB#: 3802
 Symbols: DLG1 Species: human
 Synonyms: hdlg, DLGH1, SAP97, DKFZp761P0818, DKFZp781B0426, dJ1061C18.1.1,SYNAPSE-ASSOCIATED PROTEIN 97, SAP97  Locus: 3q29 in Homo sapiens


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General Comment
General function Intracellular signaling cascade
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Cellular localization Cytoplasmic
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Ovarian function
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Expression regulated by
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Ovarian localization
Comment Cloning and characterization of E-dlg, a novel splice variant of mouse homologue of the Drosophila discs large tumor suppressor binds preferentially to SAP102. Mao P et al. Membrane-associated guanylate kinases (MAGUKs) act as scaffolds to coordinate signaling events through their multiple domains at the plasma membrane. The MAGUK SH3 domain is noncanonical and its function remains unclear. To identify potential binding partners of MAGUK SH3, the synapse-associated protein 102 (SAP102) SH3 domain was used as bait in a yeast two-hybrid screen of a mouse embryonic cDNA library. A mouse homologue of the Drosophila discs large tumor suppressor (Dlg, also known as SAP97) bound preferentially to SAP102 SH3. The 4347bp cDNA sequence encoded an 893 amino acid protein with 94% identity to mouse SAP97. A deleted region (33-aa) strongly suggests this is a novel splice variant, which we call Embryonic-dlg/SAP97 (E-dlg). The interaction of SAP102 and E-dlg was confirmed in mammalian cells. E-dlg can also bind to potassium channel Kv1.4 in a pull-down assay. E-dlg was highly expressed in embryonic and some adult mouse tissues, such as brain, kidney, and ovary. Furthermore, in situ hybridization showed that E-dlg was mostly expressed in olfactory bulb and cerebellum. (c) 2008 IUBMB IUBMB Life, 2008.
Follicle stages
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created: 2008-07-16 12:43:08 by: Aaron J Hsueh, hsuehlab   email: aaron.hsueh@stanford.edu
home page: http://reprobio.stanford.edu/hsueh
last update: 2008-07-16 12:45:04 by: Aaron J Hsueh, hsuehlab   email: aaron.hsueh@stanford.edu



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