Heat Shock Protein 90 in Human Diseases and Disorders by Alexzander A. A. Asea & Punit Kaur

Author:Alexzander A. A. Asea & Punit Kaur
Language: eng
Format: epub
ISBN: 9783030231583
Publisher: Springer International Publishing

15.1.6 R2TP-Prefoldin Complex and Additional Factors

In addition to Hsp90, the R2TP complex has also been seen to be associated with Prefoldin-like complex (PFDL) and a number of additional factors that in some cases appear to be client specific (Fig. 15.9). The PFDL consists of two subunits in common with the canonical Prefoldin complex (PFD), PFDN2 and PFDN6, as well as three other specific subunits, URI1, PDGR1 and UXT. The canonical PFD assists the folding of actin and α and β-tubulin together with the chaperone, CCT (Siegers et al. 1999; Vainberg et al. 1998). In contrast, the R2TP-PFDL complex has been implicated in snoRNPs, nuclear RNA polymerases, PIKK-containing complexes, TSC1-TSC2, TSC1-TBCD17 and the U5 snRNP complexes (Cloutier et al. 2009; Cloutier and Coulombe 2010; Cloutier et al. 2017; Izumi et al. 2012). The PFDL complex appears to consist of a complex that also contains WDR92 (also known as monad) and RBP5. It has been suggested that WDR92 can interact with RPAP3 (Itsuki et al. 2008; Sardiu et al. 2008) and that RBP5 interacts with URI (Mita et al. 2013). However, it should be noted that in S. cerevisiae the WDR2 and PFDL modules are completely absent. While this is surprising it might explain the difference between RPAP3 and the smaller Tah1p component of yeast, since RPAP3 has been implicated in the recruitment of WDR92.

Fig. 15.9Schematic showing the Hsp90-R2TP-PFDL interactions. Additionally, the interaction of the TTT complex and Prefoldin complex (PFDL-WDR92 and RBP5) is shown together with possible ZNHIT interactions that may modify the activity of the complex or help select specific clients. Other possible components include DNAAF4 (DYX1C1)-DNAAF2 (Ktu) and DNAAF4-PIH1D3 complex, which are not shown

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