Temperature and Lipid Composition Differentially Regulate KRAS Assemblies on Membranes

Abstract

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.