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Updated: May 16, 2026

Fully Processed Recombinant KRAS4b: Isolating and Characterizing the Farnesylated and Methylated Protein
Published on: January 16, 2020
Temperature and lipid composition differentially regulate KRAS assemblies on membranes
Ji Kang1, Elena Scott1, Sangho D Yun1
1Department of Chemistry, Texas A&M University, College Station, TX 77843, USA. ALaganowsky@chem.tamu.edu.
None:
RAS GTPases oligomerize on membranes to regulate signaling, but factors governing this process remain unclear. Using variable-temperature native mass spectrometry and NanoBiT assays, we show KRAS dimerization is lipid- and temperature-dependent, increasing at higher temperatures, whereas NRAS is unaffected. These results indicate entropy-driven KRAS assembly and reveal isoform-specific mechanisms of membrane organization.
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