Title : Requirement of N-terminal cysteines of PSD-95 for PSD-95 multimerization and ternary complex formation, but not for binding to potassium channel Kv1.4.

Pub. Date : 1999 Jan 1

PMID : 9867876






6 Functional Relationships(s)
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Protein Name
Organism
1 Requirement of N-terminal cysteines of PSD-95 for PSD-95 multimerization and ternary complex formation, but not for binding to potassium channel Kv1.4. Cysteine discs large MAGUK scaffold protein 4 Homo sapiens
2 Requirement of N-terminal cysteines of PSD-95 for PSD-95 multimerization and ternary complex formation, but not for binding to potassium channel Kv1.4. Cysteine discs large MAGUK scaffold protein 4 Homo sapiens
3 A pair of N-terminal cysteines, Cys3 and Cys5, is essential for the ability of PSD-95 to self-associate and to form cell surface clusters with Kv1.4. Cysteine discs large MAGUK scaffold protein 4 Homo sapiens
4 However, PSD-95 mutants lacking these cysteine residues retain their ability to associate with membranes and to bind to Kv1.4. Cysteine discs large MAGUK scaffold protein 4 Homo sapiens
5 Unlike wild type PSD-95, the cysteine mutant of PSD-95 cannot form a ternary complex with Kv1.4 and the cell adhesion molecule Fasciclin II. Cysteine discs large MAGUK scaffold protein 4 Homo sapiens
6 These results suggest that the N-terminal cysteines are essential for PSD-95 multimerization and that multimerization is required for simultaneous binding of multiple membrane protein ligands by PSD-95. Cysteine discs large MAGUK scaffold protein 4 Homo sapiens