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DAP-1, a novel protein that interacts with the guanylate kinase-like domains of hDLG and PSD-95.

Authors: Satoh, K  Yanai, H  Senda, T  Kohu, K  Nakamura, T  Okumura, N  Matsumine, A  Kobayashi, S  Toyoshima, K  Akiyama, T 
Citation: Satoh K, etal., Genes Cells. 1997 Jun;2(6):415-24.
Pubmed: (View Article at PubMed) PMID:9286858

BACKGROUND: The human homologue of the Drosophila discs large tumour suppressor protein (hDLG) and closely related proteins such as postsynaptic density protein 95 kDa (PSD-95) are associated with N-methyl-D-aspartate receptors (NMDA-R) and Shaker-type K+ channels, and are thought to be involved in their clustering. RESULTS: We have identified a protein named DAP-1 that binds to the guanylate kinase-like domains of hDLG and PSD-95. DAP-1 was found to associate with hDLG, PSD-95, NMDA-R and adenomatous polyposis coli protein (APC). Furthermore, we found that DAP-1 is specifically expressed in the brain and colocalizes with PSD-95 and APC in mouse cerebellum. We also found that DAP-1 is colocalized with PSD-95 and NMDA-R at the synapses in cultured rat hippocampal neurons. CONCLUSION: Our findings suggest that DAP-1 may play several roles in the molecular organization of synapses and neuronal cell signalling by interacting with hDLG and PSD-95, which in turn are associated with receptors, ion channels and APC.

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CRRD Object Information
CRRD ID: 8554678
Created: 2014-05-08
Species: All species
Last Modified: 2014-05-08
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.