The Networking of Chaperones by Co-chaperones

Control of Cellular Protein Homeostasis
Softcover Nachdruck of the original 1. Auflage 2015
ISBN: 978-3-319-38149-7
Verlag: Springer Nature Switzerland

Buch, Englisch, 276 Seiten, Previously published in hardcover, Format (B × H): 155 mm x 235 mm, Gewicht: 4453 g

Reihe: Subcellular Biochemistry

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.

Zielgruppe

Research

Autoren/Hrsg.

Edkins, Adrienne Lesley

Blatch, Gregory Lloyd

Fachgebiete

• Medizin | Veterinärmedizin Medizin | Public Health | Pharmazie | Zahnmedizin Vorklinische Medizin: Grundlagenfächer Molekulare Medizin, Zellbiologie
• Medizin | Veterinärmedizin Medizin | Public Health | Pharmazie | Zahnmedizin Medizin, Gesundheitswesen Biomedizin, Medizinische Forschung, Klinische Studien
• Naturwissenschaften Biowissenschaften Zellbiologie
• Naturwissenschaften Biowissenschaften Proteinforschung

Inhaltsverzeichnis

Preface
List of Contributors
About the Editors
1
GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: Nucleotide exchange factors for Hsp70 molecular chaperones
Andreas Bracher and Jacob Verghese

2
Functions of the Hsp90-Binding FKBP Immunophilins
Naihsuan Guy, Yenni A. Garcia, Jeffrey C. Sivils, Mario D. Galigniana, and Marc B. Cox

3
Hsp70/Hsp90 organising protein (Hop): beyond interactions with chaperones and prion proteins
Swati Baindur-Hudson, Adrienne L. Edkins, and Gregory L. Blatch

4
 Specification of Hsp70 function by Type I and Type II Hsp40
Douglas M. Cyr and Carlos H. Ramos

5
Cdc37 as a Co-chaperone to Hsp90
Stuart K Calderwood

6
p23 and Aha1
Alexandra B Rehn and Johannes Buchner

7
UCS proteins: chaperones for myosin and co-chaperones for Hsp90
Weiming Ni and Odutayo O. Odunuga

8
Chaperonin - Co-chaperonin Interactions
Aileen Boshoff

9
 Co-chaperones of the mammalian endoplasmic reticulum
Armin Melnyk, Heiko Rieger and Richard Zimmermann

10
The evolution and function of co-chaperones in mitochondriaNeta Regev-Rudzki, Kip Gabriel and Dejan Bursac

11
CHIP: a co-chaperone for degradation by the proteasome
Adrienne L. Edkins

12
The role of HSP70 and its co-chaperones in protein misfolding, aggregation and disease
Emma J. Duncan, Michael E. Cheetham, J. Paul Chapple, and Jacqueline van der Spuy

Index