Fig. 4
From: Structural determinants and functional consequences of protein affinity for membrane rafts
PM proteins have higher raft partitioning, and mutations of raft affinity reduced PM localization. Proteome-wide bioinformatic predictions of a palmitoylation, b TMD length, and c TMD side chain surface area reveal that all features associated with raft partitioning are predicted to be significantly enhanced in single-pass PM proteins versus a combined set of single-pass ER and Golgi proteins. d Consistently, predicted raft affinity is significantly higher for PM proteins than non-raft (3 outliers omitted for clarity). Significances are one-way ANOVA relative to PM; ***p<0.001; **p<0.01. The distribution of ΔGraft is clearly not unimodal; histogram with Gaussian fits in Supplementary Fig. 6. e–g Experimental evaluation of bioinformatics predictions. PM localization of two predicted raft proteins (LAT and PAG) was significantly reduced by mutating any of the structural features determining raft partitioning, including e palmitoylation, f TMD length, and g TMD surface area. Scale bars are 5 μm. Avg ± SD for 20–40 cells/condition. Significances are one-way ANOVA relative to the wild-type TMD; ***p<0.001; **p<0.01
