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Cell Stress and Chaperones

, Volume 22, Issue 2, pp 173–189 | Cite as

The remarkable multivalency of the Hsp70 chaperones

  • Erik R. P. Zuiderweg
  • Lawrence E. Hightower
  • Jason E. Gestwicki
Mini Review

Abstract

Hsp70 proteins are key to maintaining intracellular protein homeostasis. To carry out this task, they employ a large number of cochaperones and adapter proteins. Here, we review what is known about the interaction between the chaperones and partners, with a strong slant toward structural biology. Hsp70s in general, and Hsc70 (HSPA8) in particular, display an amazing array of interfaces with their protein cofactors. We also review the known interactions between Hsp70s with lipids and with active compounds that may become leads toward Hsp70 modulation for treatment of a variety of diseases.

Keywords

Hsc70 Protein-protein interactions Protein-drug interactions Structural biology Crystallography NMR spectroscopy 

Notes

Acknowledgements

This work was supported by NIH grant 5-R01-NS-059690-01-08.

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Copyright information

© Cell Stress Society International 2017

Authors and Affiliations

  • Erik R. P. Zuiderweg
    • 1
  • Lawrence E. Hightower
    • 2
  • Jason E. Gestwicki
    • 3
  1. 1.Department of Biological ChemistryThe University of Michigan Medical SchoolAnn ArborUSA
  2. 2.Department of Molecular and Cell BiologyUniversity of ConnecticutStorrsUSA
  3. 3.Institute for Neurodegenerative DiseaseUniversity of California at San FranciscoSan FranciscoUSA

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