Regulation of ribosomal protein S6 phosphorylation in heat-shocked HeLa cells.
Decreases in energy charge, ribosomal protein phosphorylation and rate of protein synthesis are well-documented facets of the cellular response to hyperthermia in non-vertebrates. We have tried to reproduce this response pattern in 32P-labelled HeLa cells in order to investigate the hypothetical causal relationship between these effects. In HeLa cells shifted from 36 degrees C to 42 degrees C, dephosphorylation of S6 and inhibition of protein synthesis, owing to a decreased initiation rate, were observed, but could not have been mediated by changes in the cells' general energy charge since the ATP and GTP levels were not reduced. In addition, we found that the hyperthermic translation block developed faster than the overall dephosphorylation of S6, showing that S6 dephosphorylation cannot be responsible for the translation block unless site-specific effects play a critical role.
D000255:Adenosine Triphosphate / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006160:Guanosine Triphosphate / Q000378:metabolism; D006367:HeLa Cells / Q000378:metabolism*; D006358:Hot Temperature; D006801:Humans; D008715:Methionine / Q000378:metabolism; D010766:Phosphorylation; D038601:Ribosomal Protein S6; D012269:Ribosomal Proteins / Q000378:metabolism*
D038601:Ribosomal Protein S6; D012269:Ribosomal Proteins; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate; D008715:Methionine