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The colorectal tumour suppressor APC is present in the NMDA‐receptor‐PSD‐95 complex in the brain
Author(s) -
Yanai Hiroyuki,
Satoh Kiyotoshi,
Matsumine Akihiko,
Akiyama Tetsu
Publication year - 2000
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1046/j.1365-2443.2000.00368.x
Subject(s) - nmda receptor , pdz domain , biology , adenomatous polyposis coli , microbiology and biotechnology , guanylate kinase , ampa receptor , ion channel , postsynaptic density , receptor , biochemistry , membrane protein , genetics , colorectal cancer , cancer , membrane
Background The synaptic protein PSD‐95/SAP90 interacts with ion channels such as the N‐methyl‐ D ‐aspartate‐receptor (NMDA‐R) via its PDZ domain, and is involved in their clustering. Moreover, it interacts with signalling molecules and plays an important role in coupling NMDA‐R to pathways that control synaptic plasticity and learning. Results We report that PSD‐95 interacts with the adenomatous polyposis coli (APC) tumour suppressor protein via its PDZ domain. Furthermore, we found that PSD‐95, NMDA‐R and APC are contained in the same complex in vivo . PSD‐95‐NMDA‐R–APC association was found to require two cysteine residues conserved in the amino‐terminus of PSD‐95 that are known to be critical for its multimerization. Conclusion Our findings suggest that the PSD‐95‐NMDA‐R‐APC complex forms due to the multimerization of PSD‐95 monomers, each of which can associate with either NMDA‐R or APC. It is possible that APC is involved in the regulation of ion channel clustering and/or organization of signalling molecules.