The Molecular Chaperones Interaction Networks in Protein Folding and Degradation

  • Walid A. Houry

Part of the Interactomics and Systems Biology book series (INTERACTOM, volume 1)

Table of contents

  1. Front Matter
    Pages i-xv
  2. A Global View of the Chaperone Network

    1. Front Matter
      Pages 1-1
    2. Craig Lawless, Simon J. Hubbard
      Pages 3-23
  3. Chaperones at the Ribosome

    1. Front Matter
      Pages 25-25
  4. The Hsp70 and Hsp40 Chaperone Networks

    1. Front Matter
      Pages 51-51
    2. Elizabeth A. Craig, Jaroslaw Marszalek
      Pages 53-82
    3. Veronica M. Garcia, Kevin A. Morano
      Pages 83-108
  5. The Hsp90 Chaperone Network

    1. Front Matter
      Pages 109-109
    2. Kamran Rizzolo, Philip Wong, Elisabeth R. M. Tillier, Walid A. Houry
      Pages 111-131
    3. Pablo C. Echeverria, Didier Picard
      Pages 133-149
    4. Stefan O. Ochiana, Tony Taldone, Gabriela Chiosis
      Pages 151-183
  6. The p23 Chaperone Network

    1. Front Matter
      Pages 205-205
    2. Frank J. Echtenkamp, Brian C. Freeman
      Pages 207-232
  7. Chaperone Networks in Organelles

    1. Front Matter
      Pages 233-233
    2. Pekka Maattanen, Gregor Jansen, Guennadi Kozlov, Kalle Gehring, David Y. Thomas
      Pages 235-271
    3. Johan C. Sunryd, Abla Tannous, Lydia Lamriben, Daniel N. Hebert
      Pages 273-302
    4. Wolfgang Voos, Cornelia Rüb, Michael Bruderek
      Pages 303-327
  8. The Ubiquitin-Proteasome System Network

    1. Front Matter
      Pages 329-329

About this book

Introduction

Molecular chaperones are a fundamental group of proteins that have been identified only relatively recently. They are key components of a protein quality machinery in the cell which insures that the folding process of any newly-synthesized polypeptide chain results in the formation of a properly folded protein and that the folded protein is maintained in an active conformation throughout its functional lifetime. Molecular chaperones have been shown to play essential roles in cell viability under both normal and stress conditions. Chaperones can also assist in the unfolding and degradation of misfolded proteins and in disaggregating preformed protein aggregates. Chaperones are also involved in other cellular functions including protein translocation across membranes, vesicle fusion events, and protein secretion.

In recent years, tremendous advances have been made in our understanding of the biology, biochemistry, and biophysics of function of molecular chaperones. In addition, recent technical developments in the fields of proteomics and genomics allowed us to obtain a global view of chaperone interaction networks. Finally, there is now a growing interest in the role of molecular chaperones in diseases.

This book will provide a comprehensive analysis of the structure and function of the diverse systems of molecular chaperones and their role in cell stress responses and in diseases from a global network perspective. ​

Keywords

interactomics molecular chaperones protein folding systems biology

Editors and affiliations

  • Walid A. Houry
    • 1
  1. 1.Department of BiochemistryUniversity of TorontoTorontoCanada

Bibliographic information

  • DOI https://doi.org/10.1007/978-1-4939-1130-1
  • Copyright Information Springer Science+Business Media New York 2014
  • Publisher Name Springer, New York, NY
  • eBook Packages Biomedical and Life Sciences
  • Print ISBN 978-1-4939-1129-5
  • Online ISBN 978-1-4939-1130-1
  • About this book
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