Proteomic identification of PKC-mediated expression of 20E-induced protein in Drosophila melanogaster

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Proteomic identification of PKC-mediated expression of 20E-induced protein in Drosophila melanogaster

Please use this identifier to cite or link to this item: http://hdl.handle.net/10355/3256

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Title: Proteomic identification of PKC-mediated expression of 20E-induced protein in Drosophila melanogaster
Author: Sun, Yaning; An, Shiheng; Henrich, Vincent C.; Sun, Xiaoping; Song, Qisheng
Keywords: nuclear receptor
protein expression
protein kinase
inhibitor
Date: 2007-10-09
Publisher: ACS
Citation: Journal of Proteome Research, 2007, 6 (11), pp 4478-4488
Abstract: Ecdysone receptor (EcR) and its heterodimeric partner, ultraspiracle protein (USP), are nuclear receptors that mediate the action of the insect molting hormone 20-hydroxyecdysone (20E). There is evidence that the activity of both receptors is affected by phosphorylation. Using a proteomic approach, we have shown that protein kinase C (PKC) activity is necessary for mediating 20E-induced expression of 14 specific proteins, including three previously reported 20E responsive proteins, and is also responsible for the intracellular localization of EcR and USP in larval salivary glands of Drosophila melanogaster. The 20E-dependent expression of the proteins was verified using real-time PCR and/or Western blot analysis. For some genes, inhibition of PKC activity reduced 20E-dependent transcriptional activity rapidly, raising the possibility that these are direct gene targets of EcR and USP. The data further indicate that PKC-mediated phosphorylation is also required for genes regulated indirectly by 20E-induced changes in the larval salivary gland.
URI: http://hdl.handle.net/10355/3256
ISSN: 1535-3907

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