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- W4386003707 endingPage "112047" @default.
- W4386003707 startingPage "112047" @default.
- W4386003707 abstract "The classic model of action of the glucocorticoid receptor (GR) sustains that its associated heat-shock protein of 90-kDa (HSP90) favours the cytoplasmic retention of the unliganded GR, whereas the binding of steroid triggers the dissociation of HSP90 allowing the passive nuclear accumulation of GR. In recent years, it was described a molecular machinery called transportosome that is responsible for the active retrograde transport of GR. The transportosome heterocomplex includes a dimer of HSP90, the stabilizer co-chaperone p23, and FKBP52 (FK506-binding protein of 52-kDa), an immunophilin that binds dynein/dynactin motor proteins. The model shows that upon steroid binding, FKBP52 is recruited to the GR allowing its active retrograde transport on cytoskeletal tracks. Then, the entire GR heterocomplex translocates through the nuclear pore complex. The HSP90-based heterocomplex is released in the nucleoplasm followed by receptor dimerization. Subsequent findings demonstrated that the transportosome is also responsible for the retrotransport of other soluble proteins. Importantly, the disruption of this molecular oligomer leads to several diseases. In this article, we discuss the relevance of this transport machinery in health and disease." @default.
- W4386003707 created "2023-08-20" @default.
- W4386003707 creator A5009049262 @default.
- W4386003707 creator A5023208243 @default.
- W4386003707 creator A5036948916 @default.
- W4386003707 creator A5072652265 @default.
- W4386003707 creator A5091782412 @default.
- W4386003707 date "2023-11-01" @default.
- W4386003707 modified "2023-10-07" @default.
- W4386003707 title "The transportosome system as a model for the retrotransport of soluble proteins" @default.
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