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Genes Cells. 1997 Jun;2(6):415-24.

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

Author information

  • 1Department of Oncogene Research, Institute for Microbial Diseases, Osaka University, Suita, Japan.

Abstract

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.

PMID:
9286858
[PubMed - indexed for MEDLINE]
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