Heteromultimerization and NMDA receptor-clustering activity of chapsyn-110, a member of the PSD-95 family of proteins

Chapsyn-110, a novel membrane-associated putative guanylate kinase (MAGUK) that binds directly to N-methyl-D-aspartate (NMDA) receptor and Shaker K+ channel subunits, is 70%-80% identical to, and shares an identical domain organization with, PSD-95/SAP90 and SAP97. In rat brain, chapsyn-110 protein shows a somatodendritic expression pattern that overlaps partly with PSD-95 but that contrasts with the axonal distribution of SAP97. Chapsyn-110 associates tightly with the postsynaptic density in brain, and mediates the clustering of both NMDA receptors and K+ channels in heterologous cells. Indeed, chapsyn-110 and PSD-95 can heteromultimerize with each other and are recruited into the same NMDA receptor and K, channel clusters. Thus, chapsyn-110 and PSD-95 may interact at postsynaptic sites to form a multimeric scaffold for the clustering of receptors, ion channels, and associated signalling proteins.
Publisher
CELL PRESS
Issue Date
1996-07
Language
ENG
Keywords

TUMOR-SUPPRESSOR GENE; MOLECULAR CHARACTERIZATION; SUBCELLULAR-LOCALIZATION; CHANNEL PROTEINS; K+ CHANNELS; RAT-BRAIN; SUBUNIT; HOMOLOG; NEURONS; CLONING

Citation

NEURON, v.17, no.1, pp.103 - 113

ISSN
0896-6273
DOI
10.1016/S0896-6273(00)80284-6
URI
http://hdl.handle.net/10203/73171
Appears in Collection
BS-Journal Papers(저널논문)
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