HSP 26 and 27 are phosphorylated in response to heat shock and ecdysterone in Drosophila melanogaster cells.
Protein phosphorylation has been studied in Drosophila melanogaster 8.9 K cells following heat shock. By in vivo double labelling with [35S]-methionine and [32P]-orthophosphate, we observed that two proteins are newly phosphorylated among the 26,000-27,000 dalton heat-shock proteins group. These two proteins are also phosphorylated after ecdysterone treatment, albeit at a lower level. That this phosphorylation event is induced by two different treatments, i.e. ecdysterone, a key steroid hormone of development, and heat-shock, a cellular stress suggests a possible common pathway for those two events and an important function for the phosphorylated heat-shock proteins.
D000818:Animals; D002460:Cell Line; D004331:Drosophila melanogaster / Q000378:metabolism*; D004441:Ecdysterone / Q000494:pharmacology*; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006358:Hot Temperature; D007526:Isoelectric Point; D008970:Molecular Weight; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation
D006360:Heat-Shock Proteins; D010750:Phosphoproteins; D004441:Ecdysterone