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- W2013202441 abstract "Both Ras protein and calcium play significant roles in various cellular processes via complex signaling transduction networks. However, it is not well understood whether and how Ca2+ can directly regulate Ras function. Here we demonstrate by isothermal titration calorimetry that Ca2+ directly binds to the H-Ras·GDP·Mg2+ complex with moderate affinity at the first binding site followed by two weak binding events. The results from limited proteinase degradation show that Ca2+ protects the fragments of H-Ras from being further degraded by trypsin and by proteinase K. HPLC studies together with fluorescence spectroscopic measurements indicate that binding of Ca2+ to the H-Ras·GDP·Mg2+ complex remarkably promotes guanine nucleotide exchange on H-Ras under emulated physiological Ca2+ concentration conditions. Addition of high concentrations of either of two macromolecular crowding agents, Ficoll 70 and dextran 70, dramatically enhances H-Ras guanine nucleotide exchange extent in the presence of Ca2+ at emulated physiological concentrations, and the nucleotide exchange extent increases significantly with the concentrations of crowding agents. Together, these results indicate that binding of calcium ions to H-Ras remarkably promotes H-Ras guanine nucleotide exchange under emulated physiological conditions. We thus propose that Ca2+ may activate Ras signaling pathway by interaction with Ras, providing clues to understand the role of calcium in regulating Ras function in physiological environments." @default.
- W2013202441 created "2016-06-24" @default.
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- W2013202441 date "2008-11-01" @default.
- W2013202441 modified "2023-09-23" @default.
- W2013202441 title "Binding of calcium ions to Ras promotes Ras guanine nucleotide exchange under emulated physiological conditions" @default.
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- W2013202441 doi "https://doi.org/10.1016/j.bbapap.2008.08.009" @default.
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