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Related Experiment Video

Updated: Sep 10, 2025

Author Spotlight: Advancing Cell Membrane Biophysics - Exploring Interactions and Challenges Through Experimental and Computational Approaches

Author Spotlight: Advancing Cell Membrane Biophysics - Exploring Interactions and Challenges Through Experimental and Computational Approaches

Published on: September 1, 2023

Dynamics and lipid membrane coupling of the RAS-RAF complex revealed via multiscale simulations.

Timothy S Carpenter¹, Fikret Aydin¹, Chris Neale²

¹Physical and Life Sciences (PLS) Directorate, Lawrence Livermore National Laboratory, Livermore, California.

Biophysical Journal

|August 24, 2025

Summary

Membrane environments influence RAS-RAF signaling complex formation by creating distinct lipid arrangements around RAS-RBDCRD protein complexes. These specific membrane interactions increase the probability of signaling complex assembly.

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Published on: February 17, 2023

Area of Science:

Molecular biology
Biophysics
Computational chemistry

Background:

The RAS-RAF signaling cascade is crucial for cellular processes, but its initiation mechanisms, particularly the role of membrane interactions, are not fully understood.
Understanding the interplay between membrane lipid composition and RAS/RAF protein behavior is essential for deciphering signaling pathway regulation.

Purpose of the Study:

To investigate the molecular and mechanistic insights into the initiation of the RAS-RAF signaling cascade.
To explore the complex relationship between membrane environments and RAS/RAF proteins using advanced simulation techniques.

Main Methods:

Utilized a multiscale simulation framework, Multiscale Machine-learned Modeling Infrastructure, integrating coarse-grained and all-atom molecular dynamics simulations.
Incorporated RAF RBDCRD domains into simulations alongside RAS proteins, analyzing various protein/lipid composition configurations.
Generated simulation data from micron-scale continuum simulations of hundreds of protein copies.

Main Results:

RAS-RBDCRD protein complexes on the membrane adopt distinct configurational states with unique associated lipid arrangements, forming larger "fingerprints" than RAS alone.
While strong protein complex association was observed, no statistically significant preferred protein-protein orientations were identified.
Specific membrane environments appear to facilitate spatial colocalization of RAS-RBDCRD proteins, enhancing the likelihood of signaling complex formation.

Conclusions:

Membrane composition significantly impacts the conformational states and spatial organization of RAS-RBDCRD protein complexes.
The membrane acts as a crucial modulator, increasing the probability of RAS-RAF signaling complex formation through spatial colocalization.
These findings provide novel insights into the initiation of RAS-RAF signaling at the molecular level.