Co-chaperones are important mediators of the outcome of chaperone assisted protein homeostasis, which is the dynamic integration of the processes of protein folding, degradation and translocation to ensure that cellular function is finely tuned in space and time.

Chapter 1: GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: Nucleotide exchange factors for Hsp70 molecular chaperones.- Chapter 2: Functions of the Hsp90-Binding FKBP Immunophilins.- Chapter 3: Hsp70/Hsp90 organising protein (Hop): coordinating much more than chaperones.- Chapter 4: Specification of Hsp70 function by Hsp40 Co-Chaperones.- Chapter 5: Cdc37 as a Co-chaperone to Hsp90.- Chapter 6: p23 and Aha1 - Distinct functions promote client maturation.- Chapter 7: Beyond chaperoning: UCS proteins emerge as regulators of myosin-mediated cellular processes.- Chapter 8: Chaperonin - Co-Chaperonin Interactions.- Chapter 9: Co-chaperones of the human endoplasmic reticulum: an update.- Chapter 10: J Domain Proteins Orchestrate the Multifunctionality of Hsp70s in Mitochondria: Insights from Mechanistic and Evolutionary Analyses.- Chapter 11: Impact of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity.- Chapter 12: CHIP: a co-chaperone for degradation by the proteasome and lysosome.- Chapter 13: HSP70-HSP90 chaperone networking in protein misfolding disease.