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Updated: May 28, 2025
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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
Published on: September 23, 2021
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Membrane Association of Intrinsically Disordered Proteins
Matthew MacAinsh1, Fidha Nazreen Kunnath Muhammedkutty1, Ramesh Prasad1
1Department of Chemistry, University of Illinois, Chicago, Illinois, USA;
Annual Review of Biophysics
|February 14, 2025
Summary
Intrinsically disordered proteins associate with membranes via specific motifs, regulating cellular functions. This membrane association, similar to liquid-liquid phase separation (LLPS), enables protein recruitment and membrane remodeling.
Area of Science:
- Biochemistry
- Cell Biology
- Biophysics
Background:
- Membrane association of intrinsically disordered proteins (IDPs) is crucial for cellular processes.
- IDPs regulate key functions like kinase targeting and ion channel gating.
Purpose of the Study:
- To elucidate the mechanisms driving intrinsically disordered protein membrane association.
- To explore the functional consequences of membrane-associated IDPs, including liquid-liquid phase separation (LLPS).
Main Methods:
- Residue-specific characterization using nuclear magnetic resonance (NMR) spectroscopy.
- Molecular dynamics (MD) simulations.
- Development of sequence-based prediction models for membrane association propensity.
Main Results:
- Polybasic motifs and amphipathic helices identified as primary drivers of membrane association.
- Successful prediction of residue-specific membrane association propensity.
- Demonstration that membrane association enhances protein-protein interactions and aggregation due to reduced dimensionality.
Conclusions:
- Membrane association of IDPs is a key regulatory mechanism in cellular processes.
- LLPS at membrane surfaces is a powerful mechanism for protein recruitment, clustering, and membrane remodeling.
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