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• W2767503559 startingPage "69" @default.
• W2767503559 abstract "Discs large (DLG) MAGUKs are abundantly expressed in glutamatergic synapses, crucial for synaptic transmission, and plasticity by anchoring various postsynaptic components including glutamate receptors, downstream scaffold proteins and signaling enzymes. Different DLG members have shared structures and functions, but also contain unique features. How DLG family proteins function individually and cooperatively is largely unknown. Here, we report that PSD-95 PDZ3 directly couples with SH3–GK tandem in a PDZ ligand binding-dependent manner, and the coupling can promote PSD-95 dimerization and multimerization. Aided by sortase-mediated protein ligation and selectively labeling, we elucidated the PDZ3/SH3–GK conformational coupling mechanism using NMR spectroscopy. We further demonstrated that PSD-93, but not SAP102, can also undergo PDZ3 ligand binding-induced conformational coupling with SH3–GK and form homo-oligomers. Interestingly, PSD-95 and PSD-93 can also form ligand binding-induced hetero-oligomers, suggesting a cooperative assembly mechanism for the mega-N-methyl-d-aspartate receptor synaptic signaling complex. Finally, we provide evidence showing that ligand binding-induced conformational coupling between PDZ and SH3–GK is a common feature for other MAGUKs including CASK and PALS1." @default.
• W2767503559 created "2017-11-17" @default.
• W2767503559 creator A5021163747 @default.
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• W2767503559 date "2018-01-01" @default.
• W2767503559 modified "2023-10-16" @default.
• W2767503559 title "PDZ Ligand Binding-Induced Conformational Coupling of the PDZ–SH3–GK Tandems in PSD-95 Family MAGUKs" @default.
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• W2767503559 doi "https://doi.org/10.1016/j.jmb.2017.11.003" @default.
• W2767503559 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29138001" @default.
• W2767503559 hasPublicationYear "2018" @default.
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