Hsp70-Substrate Interactions

Chapter

Abstract

The highly abundant and evolutionary conserved Hsp70 chaperones are central components of the cellular protein quality control system, surveilling the folding status of cellular proteins from birth at the ribosome to death through degradation. To no other chaperone families, more different functions have been assigned, and it is not surprising that Hsp70s are implicated in many developmental processes and pathological conditions. This versatility is due to the fact that Hsp70s bind tweezer-like degenerate motifs present in virtually all proteins, generally found in the hydrophobic core of the native conformation but exposed in the nascent state at the ribosome or translocation pores or upon stress-induced denaturation and aggregation. Recent years have seen much progress in understanding the molecular mechanism of this chaperone family. In this chapter, we review the current knowledge on structure, different conformational states, allostery, and regulation by co-chaperones in the context of Hsp70-substrate interaction.

Keywords

Chaperones Hsp70 Hsp90 Protein folding Protein degradation Protein-protein interactions Quality control Stress response 

Abbreviations

ER

Endoplasmic reticulum

Hsp

Heat shock protein

JDP

J-domain protein, also called DnaJ proteins or Hsp40

NBD

Nucleotide-binding domain

NEF

Nucleotide exchange factor

SBD

Substrate-binding domain

SBDα

α-Helical lid subdomain of the SBD

SBDβ

β-Sandwich subdomain of the SBD

UPR

Unfolded protein response

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© Springer International Publishing AG, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH-AllianceHeidelbergGermany

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