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
Population
Heterologous cells expressing PSD-95 and Kv1.4
Comparison
Mutation of N-terminal cysteines of PSD-95 vs Wild type PSD-95
Design
Preclinical
Authors
Discussion
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Member takes
Implication
N-terminal cysteines of PSD-95 enable multimerization; hypothesis-generating for cardiac Kv1.4 clustering, with no immediate clinical implications.
Structured PICO
P
Population
Heterologous cells expressing PSD-95 and Kv1.4
I
Intervention
Mutation of N-terminal cysteines (Cys3 and Cys5) of PSD-95
C
Comparator
Wild type PSD-95
O
Outcome
PSD-95 multimerization, cell surface clustering with Kv1.4, and ternary complex formationsurrogate
N-terminal cysteines of PSD-95 are essential for its multimerization and simultaneous binding of multiple membrane protein ligands, but not for binding to Kv1.4.
Cite This Study
Hsueh et al. (1999) studied this question.