Heat shock response and autophagy - cooperation and control

Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt

Standard

Heat shock response and autophagy - cooperation and control. / Dokladny, Karol; Myers, Orrin B; Moseley, Pope L.

I: Autophagy, Bind 11, Nr. 2, 2015, s. 200-213.

Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt

Harvard

Dokladny, K, Myers, OB & Moseley, PL 2015, 'Heat shock response and autophagy - cooperation and control', Autophagy, bind 11, nr. 2, s. 200-213. https://doi.org/10.1080/15548627.2015.1009776

APA

Dokladny, K., Myers, O. B., & Moseley, P. L. (2015). Heat shock response and autophagy - cooperation and control. Autophagy, 11(2), 200-213. https://doi.org/10.1080/15548627.2015.1009776

Vancouver

Dokladny K, Myers OB, Moseley PL. Heat shock response and autophagy - cooperation and control. Autophagy. 2015;11(2):200-213. https://doi.org/10.1080/15548627.2015.1009776

Author

Dokladny, Karol ; Myers, Orrin B ; Moseley, Pope L. / Heat shock response and autophagy - cooperation and control. I: Autophagy. 2015 ; Bind 11, Nr. 2. s. 200-213.

Bibtex

@article{5384305d99004822825d2242e7b6f4b8,
title = "Heat shock response and autophagy - cooperation and control",
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. ",
keywords = "Animals, Autophagy/physiology, Heat-Shock Proteins/metabolism, Heat-Shock Response/physiology, Humans, Lysosomes/metabolism, Metabolic Networks and Pathways/physiology, Signal Transduction/physiology",
author = "Karol Dokladny and Myers, {Orrin B} and Moseley, {Pope L}",
year = "2015",
doi = "10.1080/15548627.2015.1009776",
language = "English",
volume = "11",
pages = "200--213",
journal = "Autophagy",
issn = "1554-8627",
publisher = "Taylor & Francis",
number = "2",

}

RIS

TY - JOUR

T1 - Heat shock response and autophagy - cooperation and control

AU - Dokladny, Karol

AU - Myers, Orrin B

AU - Moseley, Pope L

PY - 2015

Y1 - 2015

N2 - 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.

AB - 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.

KW - Animals

KW - Autophagy/physiology

KW - Heat-Shock Proteins/metabolism

KW - Heat-Shock Response/physiology

KW - Humans

KW - Lysosomes/metabolism

KW - Metabolic Networks and Pathways/physiology

KW - Signal Transduction/physiology

U2 - 10.1080/15548627.2015.1009776

DO - 10.1080/15548627.2015.1009776

M3 - Review

C2 - 25714619

VL - 11

SP - 200

EP - 213

JO - Autophagy

JF - Autophagy

SN - 1554-8627

IS - 2

ER -

ID: 195973479