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• W2046506101 endingPage "3219" @default.
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• W2046506101 abstract "Postsynaptic density protein 95 (PSD-95/SAP-90) is a palmitoylated membrane-associated guanylate kinase that oligomerizes and clusters ion channels and associated signaling machinery at excitatory synapses in brain. However, the mechanism for PSD-95 oligomerization and its relationship to ion channel clustering remain uncertain. Here, we find that multimerization of PSD-95 is determined by only its first 13 amino acids, which also have a remarkable capacity to oligomerize heterologous proteins. Multimerization does not involve a covalent linkage but rather palmitoylation of two cysteine residues in the 13 amino acid motif. This lipid-mediated oligomerization is a specific property of the PSD-95 motif, because it is not observed with other palmitoylated domains. Clustering K+ channel Kv1.4 requires interaction of palmitoylated PSD-95 with tetrameric K+ channel subunits but, surprisingly, does not require multimerization of PSD-95. Finally, disrupting palmitoylation with 2-bromopalmitate disperses PSD-95/K+-channel clusters. These data suggest new models for K+ channel clustering by PSD-95 – a reversible process regulated by protein palmitoylation." @default.
• W2046506101 created "2016-06-24" @default.
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• W2046506101 date "2003-08-01" @default.
• W2046506101 modified "2023-10-14" @default.
• W2046506101 title "Lipid- and protein-mediated multimerization of PSD-95: implications for receptor clustering and assembly of synaptic protein networks" @default.
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• W2046506101 doi "https://doi.org/10.1242/jcs.00617" @default.
• W2046506101 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12829740" @default.
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