Abstract |
The superfamily of nuclear receptors (NRs), composed of ligand-activated transcription factors, is responsible for gene expression as a reaction to physiological and environmental changes. Transcriptional machinery may require phase separation to fulfil its role. Although NRs have a similar canonical structure, their C-terminal domains (F domains) are considered the least conserved and known regions. This article focuses on the peculiar molecular properties of the intrinsically disordered F domain of the ecdysteroid receptor from the Aedes aegypti mosquito (AaFEcR), the vector of the world's most devastating human diseases such as dengue and Zika. The His-Pro-rich segment of AaFEcR was recently shown to form the unique poly- proline helix II (PPII) in the presence of Cu2+. Here, using widefield microscopy of fluorescently labeled AaFEcR, Zn2+- and Cu2+-induced liquid-liquid phase separation (LLPS) was observed for the first time for the members of NRs. The perspectives of this finding on future research on the F domain are discussed, especially in relation to other NR members.
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Authors | Anna Więch, Aneta Tarczewska, Andrzej Ożyhar, Marek Orłowski |
Journal | Cells
(Cells)
Vol. 10
Issue 3
(03 05 2021)
ISSN: 2073-4409 [Electronic] Switzerland |
PMID | 33807814
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)
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Chemical References |
- Ions
- Receptors, Cytoplasmic and Nuclear
- Receptors, Steroid
- ecdysteroid receptor
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Topics |
- Aedes
- Animals
- Humans
- Ions
(metabolism)
- Mosquito Vectors
(pathogenicity)
- Receptors, Cytoplasmic and Nuclear
(metabolism)
- Receptors, Steroid
(metabolism)
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