Supplementary Figures S1-S18 from FH variant pathogenicity promotes purine salvage pathway dependence in kidney cancer

Supplementary Fig. S1: Analysis of FH variants and their associated interpretations of pathogenicity. Supplementary Fig. S2: Kinetic parameters for active/partially-active VUS/CI. Supplementary Fig. S3: Recombinant FH produced for 74 VUS/CI. Supplementary Fig. S4: Michaelis-Menten graphs for VUS/CI incubated with fumarate. Supplementary Fig. S5: Michaelis-Menten graphs for VUS/CI incubated with malate. Supplementary Fig. S6: Broad analysis of recombinant FH. Supplementary Fig. S7: Multimerization status of 74 VUS/CI. Supplementary Fig. S8: Tetramerization correlates with catalytic activity. Supplementary Fig. S9: Expression of FH variants in HLRCC cells. Supplementary Fig. S10: Fumarate accumulation decreases TCA intermediates. Supplementary Fig. S11: FH loss enhances de novo glutathione biosynthesis. Supplementary Fig. S12: Coessentiality of FH and nucleotide biosynthesis genes. Supplementary Fig. S13: Loss of FH activity disrupts de novo purine biosynthesis. Supplementary Fig. S14: Dysregulated purine metabolism is independent of HLRCC cell proliferation rate. Supplementary Fig. S15: FH-deficient cells use the purine salvage pathway to maintain purine nucleotide levels. Supplementary Fig. S16: Pyrimidine metabolism in FH-deficient and FH-expressing cells. Supplementary Fig. S17: Disrupting expression of purine salvage enzymes impairs tumor growth. Supplementary Fig. S18: Purine salvage inhibitor 6-mercaptopurine (6-MP) impairs tumor growth.