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.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Christopherson KS,Sweeney NT,Craven SE,Kang R,El-Husseini Ael-D,Bredt DSdoi
10.1242/jcs.00617keywords:
subject
Has Abstractpub_date
2003-08-01 00:00:00pages
3213-9issue
Pt 15eissn
0021-9533issn
1477-9137pii
116/15/3213journal_volume
116pub_type
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