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. 2015 Jan 9;7(1):49–65. doi: 10.3390/toxins7010049

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© 2015 by the authors; licensee MDPI, Basel, Switzerland.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).

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Post-dislocation scrutiny by a network of chaperones determines the cytosolic fate of RTA [38,40,81]. Following extraction from the ER by the RPT4 subunit of the proteasome, interactions with RPT5 allow RTA to recover activity. The role of Hsc70/Hsp40 interactions may be continuous scrutiny of RTA, preventing aggregation, and inactivation and activation (folding) fates follow from release of RTA from this complex. Transfer to Hsp90 via the Hsc70-Hsp90 operating protein HOP leads to CHIP-mediated ubiquitylation (Ub, ubiquitin) and inactivation of RTA. The Hsc70-interacting protein HIP stabilizes the Hsc70:RTA complex, and subsequent release by the BAG family guanine nucleotide exchange factors BAG-1 and BAG-2 leads to inactivation or folding respectively.