20-hydroxyecdysone (20E) signaling regulates amnioserosa morphogenesis during Drosophila dorsal closure: EcR modulates gene expression in a complex with the AP-1 subunit, Jun

• Main Authors: Byoungjoo Yoo, Hae-yoon Kim, Xi Chen, Weiping Shen, Ji Sun Jang, Shaianne N. Stein, Olga Cormier, Lionel Pereira, Claire R. Y. Shih, Charles Krieger, Bruce Reed, Nicholas Harden, Simon J. H. Wang
• Format: Article
• Language: English
• Published: The Company of Biologists 2021-08-01
• Series: Biology Open
• Subjects: 20-hydroxyecdysone (20e); ecdysone receptor (ecr); jun; zipper (zip); amnioserosa; dorsal closure
• Online Access: http://bio.biologists.org/content/10/8/bio058605

Steroid hormones influence diverse biological processes throughout the animal life cycle, including metabolism, stress resistance, reproduction, and lifespan. In insects, the steroid hormone, 20-hydroxyecdysone (20E), is the central hormone regulator of molting and metamorphosis, and plays roles in tissue morphogenesis. For example, amnioserosa contraction, which is a major driving force in Drosophila dorsal closure (DC), is defective in embryos mutant for 20E biosynthesis. Here, we show that 20E signaling modulates the transcription of several DC participants in the amnioserosa and other dorsal tissues during late embryonic development, including zipper, which encodes for non-muscle myosin. Canonical ecdysone signaling typically involves the binding of Ecdysone receptor (EcR) and Ultraspiracle heterodimers to ecdysone-response elements (EcREs) within the promoters of responsive genes to drive expression. During DC, however, we provide evidence that 20E signaling instead acts in parallel to the JNK cascade via a direct interaction between EcR and the AP-1 transcription factor subunit, Jun, which together binds to genomic regions containing AP-1 binding sites but no EcREs to control gene expression. Our work demonstrates a novel mode of action for 20E signaling in Drosophila that likely functions beyond DC, and may provide further insights into mammalian steroid hormone receptor interactions with AP-1.