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Impact of heterodimerization on intracellular localization of the ecdysteroid receptor (EcR)
Author(s) -
Nieva Claudia,
SpindlerBarth Margarethe,
Spindler KlausDieter
Publication year - 2008
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.20234
Subject(s) - ecdysteroid , ecdysone receptor , nuclear receptor , microbiology and biotechnology , biology , retinoid x receptor , nucleus , nuclear receptor coactivator 1 , cell nucleus , receptor , nuclear localization sequence , transcription factor , chinese hamster ovary cell , biochemistry , hormone , gene
Abstract Initially, nuclear import of the ecdysteroid receptor (EcR) in vertebrate cells (CHO‐K1 and COS‐7) does not afford a heterodimerization partner. Later on, EcR is retained in the nucleus only in the presence of a heterodimerization partner. Ultraspiracle (Usp) is more efficient compared to its vertebrate orthologue RXR and leads to an exclusively nuclear localization of EcR even in the absence of ligand. The DNA binding domain of the heterodimerization partner is important for retainment of EcR in the nucleus as shown by Usp4 (Usp R130C ), which has lost its DNA binding capability. The C‐terminal end of Usp (Usp Δ205‐508 ) encompassing the C‐terminal part of the D‐domain and the E‐ and F‐domains are essential for retainment of EcR in the nucleus. Nuclear localization is further influenced by cell‐specific factors, since hormone and heterodimerization stabilizes the EcR protein in a cell‐specific way. Arch. Insect Biochem. Physiol. 2008. © 2008 Wiley‐Liss, Inc.