6-Phosphofructo-2-kinase (PFK-2) catalyses the synthesis of fructose 2,6-bisphosphate (Fru-2,6-P2), a potent stimulator of glycolysis. In chick-embryo fibroblasts, PFK-2 activity and Fru-2,6-P2 concentration increase upon transformation by Rous sarcoma virus. We show here that the increase in PFK-2 activity required more than 2 h after shifting fibroblasts infected with a thermosensitive mutant of Rous sarcoma virus from the restrictive to the permissive temperature. Pretreatment of the cells with actinomycin D prevented this increase in PFK-2 activity, suggesting a requirement for RNA synthesis. However, the increase in PFK-2 activity did not correspond to an increase in immunoprecipitable PFK-2. Moreover, the thermostability of PFK-2 and the affinity of this enzyme for its substrate fructose 6-phosphate were increased upon transformation by Rous sarcoma virus. Staurosporine, an inhibitor of protein kinase C, prevented the increase in PFK-2 activity brought about by the shift to the permissive temperature. This, together with a comparison of the effects of phorbol esters on PFK-2 activity, suggests that pp60v-src stimulates, via protein kinase C, the transcription of a gene whose products is a distinct PFK-2 isoenzyme or a protein that activates PFK-2.
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Research Article| July 15 1992
Activation of 6-phosphofructo-2-kinase by pp60v-src is an indirect effect
M J Marchand ;
L Maisin ;
L Hue ;
Biochem J (1992) 285 (2): 413–417.
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M J Marchand, L Maisin, L Hue, G G Rousseau; Activation of 6-phosphofructo-2-kinase by pp60v-src is an indirect effect. Biochem J 15 July 1992; 285 (2): 413–417. doi: https://doi.org/10.1042/bj2850413
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