Heat shock response and autophagy--cooperation and control

Karol Dokladny, Orrin B Myers, Pope L Moseley

91 Citations (Scopus)

Abstract

Protein quality control (proteostasis) depends on constant protein degradation and resynthesis, and is essential for proper homeostasis in systems from single cells to whole organisms. Cells possess several mechanisms and processes to maintain proteostasis. At one end of the spectrum, the heat shock proteins modulate protein folding and repair. At the other end, the proteasome and autophagy as well as other lysosome-dependent systems, function in the degradation of dysfunctional proteins. In this review, we examine how these systems interact to maintain proteostasis. Both the direct cellular data on heat shock control over autophagy and the time course of exercise-associated changes in humans support the model that heat shock response and autophagy are tightly linked. Studying the links between exercise stress and molecular control of proteostasis provides evidence that the heat shock response and autophagy coordinate and undergo sequential activation and downregulation, and that this is essential for proper proteostasis in eukaryotic systems.

Original languageEnglish
JournalAutophagy
Volume11
Issue number2
Pages (from-to)200-13
Number of pages14
ISSN1554-8627
DOIs
Publication statusPublished - 2015

Keywords

  • Animals
  • Autophagy/physiology
  • Heat-Shock Proteins/metabolism
  • Heat-Shock Response/physiology
  • Humans
  • Lysosomes/metabolism
  • Metabolic Networks and Pathways/physiology
  • Signal Transduction/physiology

Fingerprint

Dive into the research topics of 'Heat shock response and autophagy--cooperation and control'. Together they form a unique fingerprint.

Cite this