Quantitative FRAP Analysis Demonstrates that Raft Protein Clustering Alters N-Ras Depalmitoylation, Membrane Interactions and Activation Pattern

Abstract

The trafficking, membrane localization and lipid raft association of oncogenic Ras proteins dictate their isoform-specific biological responses. Accordingly, their spatiotemporal dynamics are tightly regulated. While extensively studied for H- and K-Ras, such information on N-Ras, an etiological oncogenic factor, is limited. Here, we report a novel mechanism regulating the activation-dependent spatiotemporal organization of N-Ras, its modulation by biologically-relevant stimuli, and isoform-specific effects on signaling.