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

Rademacher, Nils; Kunde, Stella-Amrei; Kalscheuer, Vera M.; Shoichet, Sarah A.

doi:10.1016/j.chembiol.2013.06.016

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

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

MPS-Authors

/persons/resource/persons50369

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;

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

Rademacher.pdf
(Publisher version), 2MB

Supplementary Material (public)

There is no public supplementary material available

Citation

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: https://hdl.handle.net/11858/00-001M-0000-0018-EABB-3

Abstract

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.