Heat shock causes diverse changes in the phosphorylation of the ribosomal proteins of mammalian cells.
When HeLa cells or BHK cells were subjected to heat shock at 42 degrees C (for 2 h) or 45 degrees C (for 10 min) there was extensive dephosphorylation of ribosomal protein S6. Concomitantly ribosomal protein L14, which is not significantly phosphorylated in normal cells, became phosphorylated, as did a non-structural protein of Mr = 27000, associated with the ribosomes. The latter effects were not prevented by cycloheximide or actinomycin D. When cells shocked at 45 degrees C for 10 min were returned to 37 degrees C for 2 h there was rephosphorylation of ribosomal protein S6 and dephosphorylation of the 27 kDa protein, but not of ribosomal protein L14.
D000818:Animals; D006224:Cricetinae; D003513:Cycloheximide / Q000494:pharmacology; D003609:Dactinomycin / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006367:HeLa Cells / Q000378:metabolism; D006358:Hot Temperature; D006801:Humans; D007668:Kidney / Q000378:metabolism; D008970:Molecular Weight; D010766:Phosphorylation; D038601:Ribosomal Protein S6; D012269:Ribosomal Proteins / Q000378:metabolism*
D038601:Ribosomal Protein S6; D012269:Ribosomal Proteins; C041174:ribosomal protein L14; D003609:Dactinomycin; D003513:Cycloheximide