The Networking of Chaperones by Co-chaperones

Co-chaperones are important mediators of the outcome of chaperone assisted protein homeostasis, which is a dynamic balance between the integrated processes of protein folding, degradation and translocation. The Networking of Chaperones by Co-chaperones describes how the function of the major molecular chaperones is regulated by a cohort of diverse non-client proteins, known as co-chaperones. The second edition includes the current status of the field and descriptions of a number of novel co-chaperones that have been recently identified. This new edition has a strong focus on the role of co-chaperones in human disease and as putative drug targets. The book will be a resource for both newcomers and established researchers in the field of cell stress and chaperones, as well as those interested in cross-cutting disciplines such as cellular networks and systems biology.

This is the only book that specifically reviews the knowledge on co-chaperones as opposed to chaperones Excellent information resource for researchers entering the specialized field of cell stress and chaperones Excellent information resource for researchers in the broader field of diseases related to protein folding (e.g. Alzheimers) Includes supplementary material: sn.pub/extras

Inhalt

Preface.- List of Contributors- About the Editors- GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: Nucleotide exchange factors for Hsp70 molecular chaperones.- Functions of the Hsp90-Binding FKBP Immunophilins.- Hsp70/Hsp90 organising protein (Hop): beyond interactions with chaperones and prion proteins.- Specification of Hsp70 function by Type I and Type II Hsp40.- Cdc37 as a Co-chaperone to Hsp90.- p23 and Aha1- UCS proteins: chaperones for myosin and co-chaperones for Hsp90.- Chaperonin - Co-chaperonin Interactions.- Co-chaperones of the mammalian endoplasmic reticulum.- The evolution and function of co-chaperones in mitochondria.- CHIP: a co-chaperone for degradation by the proteasome.- The role of HSP70 and its co-chaperones in protein misfolding, aggregation and disease.- Index