Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2

Yi-Ping Hsueh, Ting-Fang Wang, Fu-Chia Yang and Morgan Sheng ()
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Yi-Ping Hsueh: Howard Hughes Medical Institute and Department of Neurobiology Massachusetts General Hospital and Harvard Medical School
Ting-Fang Wang: Howard Hughes Medical Institute and Department of Neurobiology Massachusetts General Hospital and Harvard Medical School
Morgan Sheng: Howard Hughes Medical Institute and Department of Neurobiology Massachusetts General Hospital and Harvard Medical School

Nature, 2000, vol. 404, issue 6775, 298-302

Abstract: Abstract Membrane-associated guanylate kinases (MAGUKs) contain multiple protein-binding domains that allow them to assemble specific multiprotein complexes in particular regions of the cell1,2. CASK/LIN-2, a MAGUK required for EGF receptor localization and signalling in Caenorhabditis elegans, contains a calmodulin-dependent protein kinase-like domain followed by PDZ, SH3 and guanylate kinase-like domains3,4,5. In adult rat brain, CASK is concentrated at neuronal synapses and binds to the cell-surface proteins neurexin and syndecan6,7,8 and the cytoplasmic proteins Mint/LIN-10 and Veli/LIN-7 (refs 4, 9, 10). Here we report that, through its guanylate kinase domain, CASK interacts with Tbr-1, a T-box transcription factor that is involved in forebrain development11,12. CASK enters the nucleus and binds to a specific DNA sequence (the T-element) in a complex with Tbr-1. CASK acts as a coactivator of Tbr-1 to induce transcription of T-element containing genes, including reelin, a gene that is essential for cerebrocortical development. Our findings show that a MAGUK which is usually associated with cell junctions has a transcription regulation function.

Date: 2000
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DOI: 10.1038/35005118

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