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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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.[1]

References

  1. HSP 26 and 27 are phosphorylated in response to heat shock and ecdysterone in Drosophila melanogaster cells. Rollet, E., Best-Belpomme, M. Biochem. Biophys. Res. Commun. (1986) [Pubmed]
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