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Details on Person Mineralocorticoid receptor (MR or NR3C2) is a ligand-induced...
| Class:Id | Summation:9035352 |
|---|---|
| _displayName | Mineralocorticoid receptor (MR or NR3C2) is a ligand-induced... |
| _timestamp | 2020-03-10 18:31:35 |
| created | [InstanceEdit:9035333] Shamovsky, Veronica, 2018-01-22 |
| literatureReference | [LiteratureReference:8944764] FK506-binding proteins 51 and 52 differentially regulate dynein interaction and nuclear translocation of the glucocorticoid receptor in mammalian cells [LiteratureReference:8944763] The hsp90-FKBP52 complex links the mineralocorticoid receptor to motor proteins and persists bound to the receptor in early nuclear events [LiteratureReference:9035349] Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore [LiteratureReference:8944783] Differential recruitment of tetratricorpeptide repeat domain immunophilins to the mineralocorticoid receptor influences both heat-shock protein 90-dependent retrotransport and hormone-dependent transcriptional activity [LiteratureReference:9674021] Role of molecular chaperones in steroid receptor action [LiteratureReference:9674022] The unliganded mineralocorticoid receptor is associated with heat shock proteins 70 and 90 and the immunophilin FKBP-52 [LiteratureReference:8944753] A new first step in activation of steroid receptors: hormone-induced switching of FKBP51 and FKBP52 immunophilins [LiteratureReference:9035364] Nuclear shuttling precedes dimerization in mineralocorticoid receptor signaling |
| modified | [InstanceEdit:9674018] Shamovsky, Veronica, 2020-01-10 [InstanceEdit:9676979] Shamovsky, Veronica, 2020-02-24 [InstanceEdit:9677736] Shamovsky, Veronica, 2020-03-10 |
| text | Mineralocorticoid receptor (MR or NR3C2) is a ligand-induced transcription factor, which in its unliganded state is predominantly located in the cytosol in the complex with a host cell chaperone, HSP90, and the immunophilin, FKBP5 (FKBP51) (Pratt WB et al. 2004; Bruner KL et al. 1997). Mineralocorticoid hormone aldosterone rapidly induces translocation of NR3C2 into the nucleus under physiological conditions (Grossmann C et al. 2012). Following diffusion into the cytoplasm, aldosterone binds NR3C2, induces conformational changes and replaces FKBP5 with FKBP4 (FKBP52) in the chaperone complex (Galigniana MD et al. 2010a; Davies TH et al 2002; Gallo et al. 2007). During aldosterone-induced nuclear translocation, NR3C2 remains bound to HSP90 complex both in the cytosol and the nucleus (Grossmann C et al. 2012). FKBP52 links the NR3C2:HSP90 complex to dynein/dynactin motors favoring transport of the cytoplasmic NR3C2 (MR) to the nucleus (Wochnik GM et al. 2005; Gallo LI et al. 2007). By contrast, FKBP51, which does not bind dynein and negatively regulates NR3C2 (MR) action, dissociates from the NR3C2:HSP90 chaperone complex upon aldosterone binding so as to permit the recruitment of FKBP52 (Galigniana MD et al. 2010a,b; Gallo LI et al. 2007). In the nucleus, HSP90 dissociates from NR3C2, which then forms homodimers and binds to DNA (Grossmann C et al. 2012). Like other transcription factors, NR3C2 is not confined to any particular compartment but continuously shuttles between the cytoplasm and the nucleus. A similar differential regulation of dynein interaction by FKBP51 and FKBP52 has also been demonstrated for the glucocorticoid receptor (GR) (Wochnik GM et al. 2005). The Reactome event shows the microtubule-associated nuclear translocation of NR3C2 (MR) through the recruitment of the large immunophilin FKBP52 (FKBP4) to the chaperone HSP90 complex (Galigniana MD et al. 2010a, b). |
| (summation) | [BlackBoxEvent:9035340] HSP90:ATP:FKBP4:PTGES3:NR3C2:NR3C2 ligand translocates to the nucleus [Homo sapiens] [BlackBoxEvent:9605352] HSP90:ATP:FKBP4:PTGES3:NR3C1:NR3C1 ligand translocates to the nucleus [Homo sapiens] |
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No pathways have been reviewed or authored by Mineralocorticoid receptor (MR or NR3C2) is a ligand-induced... (9035352)
