Evolution of the thyroid hormone, retinoic acid, ecdysone and liver X receptors | Zendy

Noah Ollikainen | Zendy; Charlie Chandsawangbhuwana | Zendy; Michael E. Baker | Zendy

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Evolution of the thyroid hormone, retinoic acid, ecdysone and liver X receptors

Author(s) -

Noah Ollikainen,

Charlie Chandsawangbhuwana,

Michael E. Baker

Publication year - 2006

Publication title -

integrative and comparative biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.328

H-Index - 123

eISSN - 1557-7023

pISSN - 1540-7063

DOI - 10.1093/icb/icl035

Subject(s) - ecdysone receptor , thyroid hormone receptor , nuclear receptor , thyroid hormone receptor beta , thyroid hormone receptor alpha , retinoid x receptor , retinoic acid , medicine , biology , endocrinology , thyroid , retinoic acid receptor , hormone , ecdysone , receptor , retinoid x receptor gamma , liver x receptor , hormone receptor , transcription factor , biochemistry , genetics , gene , cancer , breast cancer

Ecdysone and thyroid hormone are 2 ligands that have important roles in regulating metamorphosis in animals. Ecdysone is a steroid that regulates molting in insects. Thyroid hormone regulates differentiation and development in fish and amphibia. Although ecdysone and thyroid hormone have different chemical structures, both hormones act by binding to transcription factors that belong to the nuclear receptor family. We investigated the evolution of structure and function in the ecdysone receptor (EcR) and thyroid hormone receptor (TR), and liver X receptor (LXR) and retinoic acid receptor (RAR), which cluster with EcR and TR, respectively (Bertrand S, Brunet FG, Escriva H, Parmentier G, Laudet V, Robinson-Rechavi M. 2004. Mol Biol Evol 21:1923-37), by constructing a multiple alignment of their sequences and calculating ancestral sequences for TR, RAR, EcR, and LXR. These alignments were mapped onto the 3D structures of TR, RAR, EcR, and LXR in the Protein Data Bank to examine the evolution of amino acids involved in the binding of ligands to TR, RAR, EcR, and LXR.

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