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Synaptic MAGUK multimer formation is mediated by PDZ domains and promoted by ligand binding

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Kalscheuer,  Vera M.
Chromosome Rearrangements and Disease (Vera Kalscheuer), Dept. of Human Molecular Genetics (Head: Hans-Hilger Ropers), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Zitation

Rademacher, N., Kunde, S.-A., Kalscheuer, V. M., & Shoichet, S. A. (2013). Synaptic MAGUK multimer formation is mediated by PDZ domains and promoted by ligand binding. Chemistry & Biology, 20(8), 1044-1054. doi:10.1016/j.chembiol.2013.06.016.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0018-EABB-3
Zusammenfassung
To examine the scaffolding properties of PSD-95, we have taken advantage of established ligand/PDZ domain interactions and developed a cell-based assay for investigating protein complex formation. This assay enables quantitative analysis of PDZ domain-mediated protein clustering using bimolecular fluorescence complementation (BiFC). Two nonfluorescent halves of EYFP were fused to C-terminal PDZ ligand sequences to generate probes that sense for PDZ domain binding grooves of adjacent (interacting) molecules. When these probes are brought into proximity by the PDZ domains of a multiprotein scaffold, a functional fluorescent EYFP molecule can be detected. We have used this system to examine the properties of selected PSD-95 variants and thereby delineated regions of importance for PSD-95 complex formation. Further analysis led to the finding that PSD-95 multimerization is PDZ domain-mediated and promoted by ligand binding.