H Yanai1, K Satoh, A Matsumine, T Akiyama. 1. Laboratory of Molecular and Genetic Information, Institute for Molecular and Cellular Biosciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113, Japan.
Abstract
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.
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.
Authors: Erik I Charych; Barbara F Akum; Joshua S Goldberg; Rebecka J Jörnsten; Christopher Rongo; James Q Zheng; Bonnie L Firestein Journal: J Neurosci Date: 2006-10-04 Impact factor: 6.167
Authors: Antonella Pirone; Jonathan Alexander; Lauren A Lau; David Hampton; Andrew Zayachkivsky; Amy Yee; Audrey Yee; Michele H Jacob; Chris G Dulla Journal: Neurobiol Dis Date: 2016-11-13 Impact factor: 5.996
Authors: J L Mohn; J Alexander; A Pirone; C D Palka; S-Y Lee; L Mebane; P G Haydon; M H Jacob Journal: Mol Psychiatry Date: 2014-06-17 Impact factor: 15.992