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Details on Person Steroid hormone receptors (SHRs) are shuttling proteins, whi...
| Class:Id | Summation:8944779 |
|---|---|
| _displayName | Steroid hormone receptors (SHRs) are shuttling proteins, whi... |
| _timestamp | 2017-02-21 00:24:22 |
| created | [InstanceEdit:8944766] Shamovsky, Veronica, 2016-11-04 |
| literatureReference | [LiteratureReference:8944754] Binding of hsp90-associated immunophilins to cytoplasmic dynein: direct binding and in vivo evidence that the peptidylprolyl isomerase domain is a dynein interaction domain [LiteratureReference:8944763] The hsp90-FKBP52 complex links the mineralocorticoid receptor to motor proteins and persists bound to the receptor in early nuclear events [LiteratureReference:8944749] FKBP52 [LiteratureReference:8944764] FK506-binding proteins 51 and 52 differentially regulate dynein interaction and nuclear translocation of the glucocorticoid receptor in mammalian cells [LiteratureReference:8944753] A new first step in activation of steroid receptors: hormone-induced switching of FKBP51 and FKBP52 immunophilins [LiteratureReference:8944782] Importin 7 and importin alpha/importin beta are nuclear import receptors for the glucocorticoid receptor [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:8944759] Evidence that the FK506-binding immunophilin heat shock protein 56 is required for trafficking of the glucocorticoid receptor from the cytoplasm to the nucleus [LiteratureReference:8944769] Two signals mediate hormone-dependent nuclear localization of the glucocorticoid receptor [LiteratureReference:8944785] Evidence for glucocorticoid receptor transport on microtubules by dynein [LiteratureReference:8979032] Nuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin beta |
| modified | [InstanceEdit:8948989] Shamovsky, Veronica, 2016-11-19 [InstanceEdit:8957326] Shamovsky, Veronica, 2017-01-24 [InstanceEdit:8979033] Shamovsky, Veronica, 2017-02-21 |
| text | Steroid hormone receptors (SHRs) are shuttling proteins, which continuously undergo nuclear import and export. Although the various SHRs have different resting localizations in cells, rapid and almost complete nuclear translocation following ligand addition is a common behavior observed for almost all SHRs (except the already nuclear estrogen receptors). The Reactome event shows microtubule-associated nuclear translocation through the recruitment of the large immunophilin FKBP52 (FKBP4) to the SHR:HSP90 complex (Galigniana et al. 2002; Wochnik et al. 2005; Davies and Sanchez 2005; Galigniana MD et al. 2010). FKBP52 links glucocorticoid receptor (GR):HSP90 and mineralocorticoid receptor (MR):HSP90 complexes to dynein/dynactin motors favoring transport of the cytoplasmic SHR to the nucleus (Wochnik et al. 2005; Gallo L et al. 2007). Moreover, the cytoplasmic-nuclear movement of GR was blocked in fibroblasts co-expressing dynamitin, which dissociates dynein from its cargoes (Harrell et al. 2004). FKBP52 directly binds to the motor protein dynein through the peptidyl-prolyl isomerase (PPIase) domain (Wochnik et al. 2005). Interestingly, the PPIase domain of another immunophilin FKBP51 (FKBP5) is unable to interact with dynein. Without hormone, FKBP51 is the major immunophilin in GR:HSP90 complexes, whereas after hormone treatment, FKBP52 rapidly replaces FKBP51 such that these complexes are now able to translocate to the nucleus with an accelerated rate (Davies et al. 2002). In addition, replacement of FKPB52 by FKBP51 favored the cytoplasmic localization of MR (Galigniana MD et al. 2010). On the other hand, GR was apparently able to translocate to the nucleus with the same rate even if the microtubule network was completely disrupted suggesting that he subcellular localization of SHRs can be controlled by several coexisting mechanisms (Czar et al. 1995). Indeed, in yeast and mammalian cells liganded and unliganded SHRs can bind several importins to be translocated into the nucleus (Freedman & Yamamoto 2004; Picard & Yamamoto 1987). In addition, importin beta and the integral nuclear pore glycoprotein NUP62 interact with HSP90, HSP70, p23, and the TPR domain proteins FKBP52 and PP5. NUP62 and GR are able to interact in a more efficient manner when chaperoned by the HSP90-based heterocomplex (Echeverria et al. 2009). GR cross-linked to the HSP90 heterocomplex is able to translocate to the nucleus in digitonin-permeabilized cells treated with steroid, suggesting that GR could pass through the pore in its untransformed state (Echeverria et al. 2009). |
| (summation) | [BlackBoxEvent:5618080] HSP90:ATP:p23:FKBP52:SHR:SH translocates to the nucleus [Homo sapiens] |
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No pathways have been reviewed or authored by Steroid hormone receptors (SHRs) are shuttling proteins, whi... (8944779)
