Table 2.
Major redox modifications on oncogenic Ras protein.
| Ras isoform | Inducer | Chemical modification | Method | Cell type | Phenotypic read-out | References |
|---|---|---|---|---|---|---|
| KRASG12C (Gly12→Cys) | RNS (NO) | S-Nitrosylation (Cys12) | Biochemical analysis | Human Lung | Tumorigenic activity | [55] |
| KRASC118S (Cys118→Ser) | – | – | Tumour xenograft analysis Biochemical analysis |
Mouse Lung | Decreased tumorigenesis | [56] |
| KRASC118S (Cys118→Ser) | – | – | Tumour xenograft analysis Biochemical analysis |
Mouse Lung | Decreased tumorigenesis | [57] |
|
NRASG12C (Gly12→Cys) HRASG12V (Gly12→Val) |
Retroviral expression | – | Cell survival, proliferation, and cell-cycle analysis | Human haematopoietic progenitors | Increased proliferation | [58] |
Footnote: Cysteine residues sites of redox modification are listed in the table with principal redox-inducer and experimental model specifications (reactive oxygen or nitrogen species; type of chemical modification; phenotypic cellular read-outs; analytical methods). This list focuses on aspects relevant to the current paper and is not intended to be truly comprehensive. a No effects means no measurable effect on the protein structure, GTPase activity, intrinsic and GEF-mediated guanine nucleotide dissociation rate, or the ability to bind an effector; b The recombinant p21ras was obtained from BioMol (Plymouth Meeting, PA).