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Related Experiment Video

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Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

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Published on: January 5, 2024

Intramolecular domain dynamics regulate synaptic MAGUK protein interactions.

Nils Rademacher¹, Benno Kuropka², Stella-Amrei Kunde¹

¹Neuroscience Research Center, Charité-Universitätsmedizin Berlin, Berlin, Germany.

|March 14, 2019

Summary

Binding of CRIPT-derived ligands to PSD-95 (postsynaptic density-95) scaffold proteins alters its structure, enabling new interactions. This reveals a hierarchical mechanism for assembling synaptic protein complexes, including the G protein subunit Gnb5.

Keywords:

MAGUK bimolecular fluorescence complementation biochemistry chemical biology heterotrimeric G protein subunit neuroscience postsynaptic density protein complex regulation quantitative mass spectrometry rat

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Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

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Published on: August 21, 2019

Area of Science:

Neuroscience
Molecular Biology
Biochemistry

Background:

Postsynaptic density-95 (PSD-95) is a MAGUK family scaffold protein crucial for organizing synaptic transmission.
Its multi-domain structure, featuring PDZ and SH3-GK domains, facilitates the assembly of protein complexes at synapses.

Purpose of the Study:

To investigate how ligand binding to PSD-95's PDZ domains influences its intramolecular structure and subsequent complex formation.
To identify novel PSD-95 interactors and elucidate the hierarchical mechanism of PSD-95 complex assembly.

Main Methods:

Utilized CRIPT-derived PDZ3 ligands to probe PSD-95 structure-function relationships.
Employed biochemical assays to identify and characterize PSD-95 interactors.
Investigated protein complex formation in rat hippocampal neurons.

Main Results:

Binding of PDZ3 ligands to PSD-95's third PDZ domain induces conformational changes in the SH3-GK tandem domain.
Identified context-dependent binding of PSD-95 interactors to the SH3-GK domain.
Established Gnb5 (G protein subunit beta 5) as a PSD-95 interactor at dendritic spines, with binding mediated by the PSD-95 GK domain and triggered by PDZ3 ligand interaction.

Conclusions:

PSD-95 complex formation is regulated by a hierarchical binding mechanism initiated by ligand engagement with PDZ domains.
Conformational changes in PSD-95 dictate its interaction with downstream partners like Gnb5, influencing synaptic organization.