Abstract
Phosphorylation of a 38 kDa protein (p38) present in rat liver plasma membrane has been shown for the first time to be enhanced by ras proteins. This increase in phosphorylation is about 3–16-fold depending on the incubation time and the type of ras protein used. Acid treatment removes phosphate from this protein suggesting that the phosphorylation involves phosphoramidate derivatives of basic amino acids. Experiments carried out in the presence of diethylpyrocarbonate suggest that the phosphorylation occurs on (a) histidine residue(s). It is probable that the function of p38 in the cell is modulated by ras proteins through phosphorylation. The significance of phosphorylation of p38 in terms of malignant transformation is presently unknown.
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