Cancer-associated arginine-to-histidine mutations confer a gain in pH sensing to mutant proteins

• DOI: 10.1126/scisignal.aam9931
• Publication Date: 2017-09-05T18:20:32Z
• Authors: Katharine A. White; Diego Garrido Ruiz; Zachary A. Szpiech; Nicolas B. Strauli; Ryan D. Hernandez; Matthew P. Jacobson; Diane L. Barber
• Keywords: 0301 basic medicine; Carcinogenesis; Protein Conformation; Bioinformatics and Computational Biology; 610; Breast Neoplasms; Arginine; 03 medical and health sciences; Breast Cancer; Genetics; Tumor Cells, Cultured; 2.1 Biological and endogenous factors; Humans; Histidine; Aetiology; Cancer; Cell Proliferation; Cultured; Biological Sciences; Hydrogen-Ion Concentration; Tumor Cells; 3. Good health; ErbB Receptors; Biochemistry and cell biology; Mutation; Women's Health; Female; Biochemistry and Cell Biology; Tumor Suppressor Protein p53

High intracellular pH in cancer cells enables the oncogenic effects of Arg-to-His mutations proteins.