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Journal Article

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


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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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.

Cite as: http://hdl.handle.net/11858/00-001M-0000-0018-EABB-3
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.