HSP 26 and 27 are phosphorylated in response to heat shock and ecdysterone in Drosophila melanogaster cells

Abstract

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.