Nucleocytoplasmic Shuttling of Steroid Receptors
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Cited by (83)
The role of glucocorticoid receptors in metabolic syndrome and psychiatric illness
2017, Journal of Steroid Biochemistry and Molecular BiologyCitation Excerpt :However, GR trafficking from the cytoplasm to the nucleus is bidirectional. The ability of the receptor to translocate back and forth [13] is primarily regulated by proteins that serve as cytoplasmic anchors (molecular chaperones, dynein, and 14-3-3 proteins) [14,15]. Additionally, in vitro studies have also shown that c-Jun N-terminal kinase (JNK), can enhance nuclear expulsion of GR limiting its transactivation properties [16].
Interplay of estrogen receptors and FOXA factors in the liver cancer
2015, Molecular and Cellular EndocrinologyCitation Excerpt :In ERα, the AF1 is constitutively active and AF2 is ligand-dependent, while the function of AF1 in ERβ is weaker than that in ERα, so the transcriptional activation of ERβ depends more on ligand-dependent AF2 domains (Delaunay et al., 2000). Both ERα and ERβ can shuttle between the cytoplasm and nucleus (Defranco et al., 1995; Tyagi et al., 1998). In addition, another membrane-associated estrogen receptor, GPER (also known as GPR30), was discovered in 2000 (Filardo et al., 2000), and the GPER1 gene has been cloned and investigated in several labs (Carmeci et al., 1997; Feng and Gregor, 1997; Kvingedal and Smeland, 1997; O’Dowd et al., 1998).
Glucocorticoid receptor concentration and the ability to dimerize influence nuclear translocation and distribution
2013, SteroidsCitation Excerpt :The unliganded GR, although mostly cytoplasmic, does exist in a dynamic equilibrium where a small proportion of the population is actively shuttled into the nucleus and allowed to diffuse back into the cytoplasm. Upon ligand activation this equilibrium shifts toward a predominantly import driven state, which results in a primarily nuclear localization of the GR [27,65]. Thus, the degree of nuclear localization reflects both the rate of nuclear import as well as the rate of nuclear export [53].
Molecular chaperones, essential partners of steroid hormone receptors for activity and mobility
2010, Biochimica et Biophysica Acta - Molecular Cell ResearchRole of hsp90 and the hsp90-binding immunophilins in signalling protein movement
2004, Cellular SignallingStructure and Function of the Glucocorticoid Receptor Ligand Binding Domain
2004, Vitamins and HormonesCitation Excerpt :One model suggests that ligand binding induces the release of the bound chaperone partners, consequently exposing the nuclear localization sites within the GR LBD. However, the role of hsp partners is probably much more complex, because they have also been implicated in aiding transport and cytoplasmic nuclear shuttling of GR (Defranco et al., 1995; Pratt, 1993) and also participating in an active role within the transcriptional complex (Freeman et al., 2000). Another consequence following ligand association is the formation of either receptor homodimers or heterodimers with related NRs (Savory et al., 2001).