Co-chaperones

Co-chaperones of Hsp60 Prefold in (GimC) - Cpn10 (mtHspIO)... 

Connell, P., et al.. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat Cell Biol, 2001, 3(1), 93-6. 

Chaperones are connected to proteasomes in at least four ways. First, chaperones can deliver substrates to the proteasome as described above for the co-chaperone... 

Meacham, G. C., C. Patterson, W. Zhang, J. M. Younger, and D. M. Cyr. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat Cell Biol. 3 100-5.2001. 

Many of the chaperones double as heat shock-proteins (Hsp). When a cell is put under stress that can cause proteins to denature, such as too high a temperature, it produces heat-shock proteins. Their names are abbreviated to Hsp plus their subunit molecular mass in kDa. Hsp70, for example, is a ubiquitous heat-shock protein in eukaryotes. It is known in E. coli as DnaK for historical reasons because it was first discovered from a supposed role in DNA replication. Hsp70 is also important in protein trafficking and the conveying of proteins across membranes, because the denatured state is important in these processes. In protein biosynthesis, the unfolded state of the nascent polypeptide chain is passed on to DnaK, which maintains it in an extended form. The chain, under the influence of ATP and co-chaperones such as DnaJ and GrpE, is handed over to GroEL. 

Panaretou, B. et al. 2002. Activation of the ATPase activity of hsp90 by the stress-regulated co-chaperone ahal. Mol. Cell 10, 1307-1318. 

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