Disulfide-linked head-to-head multimerization in the mechanism of ion channel clustering by PSD-95

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The PSD-95/SAP90 family of PDZ-containing proteins is directly involved in the clustering of specific ion channels at synapses. We report that channel clustering depends on a conserved N-terminal domain of PSD-95 that mediates multimerization and disulfide linkage of PSD-95 protomers. This N-terminal multimerization domain confers channel clustering activity on a single PDZ domain. Thus, channel clustering depends on aggregation of PDZ domains achieved by head-to-head multimerization of PSD-95, rather than by concatenation of PDZ domains in PSD-95 monomers. This mechanism predicts that PSD-95 can organize heterogeneous membrane protein clusters via differential binding specificities of its three PDZ domains. PSD-95 and its relative chapsyn-110 exist as disulfide-linked complexes in rat brain, consistent with head-to-head multimerization of these proteins in vivo.
Publisher
CELL PRESS
Issue Date
1997-05
Language
English
Article Type
Article
Keywords

TUMOR-SUPPRESSOR PROTEIN; GUANYLATE KINASES; K+ CHANNELS; SYNAPSES; HOMOLOG; SAP90

Citation

NEURON, v.18, no.5, pp.803 - 814

ISSN
0896-6273
DOI
10.1016/S0896-6273(00)80319-0
URI
http://hdl.handle.net/10203/73971
Appears in Collection
BS-Journal Papers(저널논문)
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