AI Article Synopsis
- The postsynaptic density (PSD) is a crucial protein assembly in neurons that relies on specific protein-protein interactions for its structure and function.
- This research identifies a key peptide involved in the liquid-liquid phase separation (LLPS) of PSD-95, particularly through its interaction with Stargazin (a transmembrane AMPA receptor regulatory protein).
- The study highlights that the formation of LLPS can be influenced by the presence of pharmacological inhibitors and underscores the significance of both multivalent interactions and short, charged peptides in promoting LLPS in complex protein systems.
Article Abstract
The organization of the postsynaptic density (PSD), a protein-dense semi-membraneless organelle, is mediated by numerous specific protein-protein interactions (PPIs) which constitute a functional postsynapse. The PSD protein 95 (PSD-95) interacts with a manifold of proteins, including the C-terminal of transmembrane AMPA receptor (AMPAR) regulatory proteins (TARPs). Here, we uncover the minimal essential peptide responsible for the Stargazin (TARP-γ2)-mediated liquid-liquid phase separation (LLPS) formation of PSD-95 and other key protein constituents of the PSD. Furthermore, we find that pharmacological inhibitors of PSD-95 can facilitate the formation of LLPS. We found that in some cases LLPS formation is dependent on multivalent interactions, while in other cases short, highly charged peptides are sufficient to promote LLPS in complex systems. This study offers a new perspective on PSD-95 interactions and their role in LLPS formation, while also considering the role of affinity over multivalency in LLPS systems.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8844826 | PMC |
| http://dx.doi.org/10.1016/j.isci.2022.103808 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!