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Comment
. 2010 Aug 13;329(5993):766-7.
doi: 10.1126/science.1194160.

Cell Biology. The proteome in balance

Darren Hutt  1 , William E Balch
Affiliations
Comment

Cell Biology. The proteome in balance

Darren Hutt et al. Science. .
No abstract available

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Figures

Figure 1
Figure 1. The Yin and Yang of proteostasis
Schematic representation of the balance between the folding (Yang) and degradation (Yin) branches of the cellular proteostasis network (PN) that globally manage protein folding in the cell in health and disease. Hsp70 and Hsp90, core components of the PN, are cycled between active and inactive forms by regulatory co-chaperones. The ATP bound, client binding competent state of Hsp90 (Hsp90A) is stabilized by p23, a step involved in protein folding. The release of clients is accomplished by inactivation of the Hsp90 (Hsp90I) through activation of its ATPase activity, which is regulated by Aha1. The active, client binding competent state of Hsp70 (Hsp70A) is the ADP bound state, which is generated by DNAJ family of (Hsp40) proteins, which are ATPase activating co-chaperones. Client release is achieved either by transfer of the client to Hsp90 via the activity of Hsp70/90 organizing protein (HOP) or by BAG/TRP-domain containing proteins. BAG proteins mediate the ADP/ATP exchange of Hsp70. Prolonged binding of clients to Hsp70 results in the recruitment of E2 ubiquitin conjugating and E3 ubiquitin ligating enzymes leading to degradative pathways. UbcH5 and CHIP are the respective enzymes mediating the ubiquitination and ER-associated degradation or lysosomal delivery of CFTR (Okiyoneda et al. REF).
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