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EMBO reports 2, 10, 885–890 (2001)
doi:10.1093/embo-reports/kve206
Figure 3
From the cradle to the grave: molecular chaperones that may choose between folding and degradation
Jörg Höhfeld, Douglas M. Cyr & Cam Patterson
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| Model for Hsp70 chaperone machines. Binding of distinct chaperone cofactors to the N-terminal ATPase domain of Hsp70 (ATPase) and to its C-terminus (C) may give rise to chaperone machines involved in protein folding and protein degradation, respectively. The cofactors Hip and BAG-1 compete for binding to the ATPase domain, while Hop and CHIP associate with the C-terminus in a competitive manner. During folding and degradation, Hsp70 appears to co-operate with cofactors of the Hsp40 protein family. pep., peptide binding domain of Hsp70; ubl, ubiquitin-like domain of BAG-1; U, U-box of CHIP.
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