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Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain

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Positive cooperativity between RAS-binding and cysteine-rich domains regulates RAF membrane binding kinetics via

Andres Jimenez Salinas¹, Kesaria Tevdorashvili¹, Julian Grim¹

¹Department of Chemistry and Biochemistry, San Diego State University, San Diego, CA, USA.

Nature Communications

|February 10, 2026

Summary

RAF activation relies on coordinated RAS and lipid interactions. This study reveals how these interactions stabilize RAF on membranes, promoting its multistep activation via sustained membrane retention.

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Area of Science:

Molecular biology
Cell signaling
Biophysics

Background:

RAF activation is crucial for cellular signaling pathways.
The precise molecular mechanisms governing RAF's membrane recruitment and activation by RAS and lipids are not fully understood.

Purpose of the Study:

To elucidate the molecular basis of RAF activation through coordinated protein-protein and protein-lipid interactions.
To investigate the role of membrane environments in regulating RAF binding dynamics and activation.

Main Methods:

Utilized a bottom-up reconstitution approach to study RAF-RAS-lipid interactions.
Investigated the cooperative binding of RAF domains (RBD and CRD) within membrane environments.

Main Results:

Demonstrated cooperativity between RAF's RAS-binding domain (RBD) and cysteine-rich domain (CRD) for membrane stabilization.
Showed that CRD-mediated phosphatidylserine binding stabilizes the RBD:RAS complex.
Identified lateral rebinding to RAS as a key mechanism for sustained RAF membrane retention, facilitated by weak CRD-lipid interactions.

Conclusions:

Coordinated protein-protein and protein-lipid interactions are essential for regulating RAF membrane binding dynamics and multistep activation.
Lateral rebinding extends RAF's membrane dwell time, potentially facilitating complete activation.
Sustained membrane retention through weak multivalent interactions may be a common regulatory mechanism for signaling proteins.