Heat shock response and autophagy--cooperation and control

Autor: Pope L. Moseley, Karol Dokladny, Orrin Myers
Rok vydání: 2015
Předmět:
protein synthesis
BECN1
Beclin 1
autophagy related

NR1D1/Rev-Erb-α
nuclear receptor subfamily 1
group D
member 1

Review
AKT
v-akt murine thymoma viral oncogene homolog 1

Lysosomes/metabolism
ATG
autophagy-related

FOXO
forkhead box O

Heat-Shock Proteins
HSP70
AMPK
adenosine monophosphate-activated protein kinase

exercise
PPARGC1A/PGC-1α
peroxisome proliferator-activated receptor
gamma
coactivator 1 α

protein breakdown
Cell biology
Biochemistry
MTMR14/hJumpy
myotubularin related protein 14

Protein folding
HSP
heat shock protein

Autophagy/physiology
Metabolic Networks and Pathways
Signal Transduction
autophagy
PBMC
peripheral blood mononuclear cell

MTOR
mechanistic target of rapamycin

Protein degradation
Biology
ER
endoplasmic reticulum

heat shock response
RHEB
Ras homolog enriched in brain

Heat shock protein
SOD
superoxide dismutase

EIF4EBP1
eukaryotic translation initiation factor 4E binding protein 1

Animals
Humans
Heat shock
HSPA8/HSC70
heat shock 70kDa protein 8

Molecular Biology
SQSTM1/p62
sequestosome 1

LC3
MAP1LC3
microtubule-associated protein 1 light chain 3

Heat-Shock Response/physiology
Signal Transduction/physiology
Autophagy
Heat-Shock Proteins/metabolism
Cell Biology
Hsp70
IL
interleukin

ULK1
unc-51 like autophagy activating kinase 1

TPR
translocated promoter region
nuclear basket protein

Proteostasis
Proteasome
HSF1
heat shock transcription factor 1

Lysosomes
TSC
tuberous sclerosis complex

Metabolic Networks and Pathways/physiology
Heat-Shock Response
Zdroj: Autophagy
Dokladny, K, Myers, O B & Moseley, P L 2015, ' Heat shock response and autophagy-cooperation and control ', Autophagy, vol. 11, no. 2, pp. 200-213 . https://doi.org/10.1080/15548627.2015.1009776
ISSN: 1554-8635
Popis: 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.
Databáze: OpenAIRE