The role of AMP-activated protein kinase in the coordination of skeletal muscle turnover and energy homeostasis

The AMP-activated protein kinase (AMPK) is a serine/threonine protein kinase that acts as a sensor of cellular energy status switch regulating several systems including glucose and lipid metabolism. Recently, AMPK has been implicated in the control of skeletal muscle mass by decreasing mTORC1 activi...

Celý popis

Uložené v:
Podrobná bibliografia
Vydané v:American Journal of Physiology: Cell Physiology Ročník 303; číslo 5; s. C475
Hlavní autori: Sanchez, Anthony M J, Candau, Robin B, Csibi, Alfredo, Pagano, Allan F, Raibon, Audrey, Bernardi, Henri
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: United States 01.09.2012
Predmet:
AMP-Activated Protein Kinases - genetics
AMP-Activated Protein Kinases - metabolism
Animals
Energy Metabolism - physiology
Gene Expression Regulation, Enzymologic - physiology
Humans
Muscle, Skeletal - enzymology
Muscle, Skeletal - metabolism
ISSN:1522-1563, 1522-1563
On-line prístup:Zistit podrobnosti o prístupe
Tagy: Pridať tag
Žiadne tagy, Buďte prvý, kto otaguje tento záznam!
Popis
Shrnutí:The AMP-activated protein kinase (AMPK) is a serine/threonine protein kinase that acts as a sensor of cellular energy status switch regulating several systems including glucose and lipid metabolism. Recently, AMPK has been implicated in the control of skeletal muscle mass by decreasing mTORC1 activity and increasing protein degradation through regulation of ubiquitin-proteasome and autophagy pathways. In this review, we give an overview of the central role of AMPK in the control of skeletal muscle plasticity. We detail particularly its implication in the control of the hypertrophic and atrophic signaling pathways. In the light of these cumulative and attractive results, AMPK appears as a key player in regulating muscle homeostasis and the modulation of its activity may constitute a therapeutic potential in treating muscle wasting syndromes in humans.
Bibliografia:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
ObjectType-Review-3
content type line 23
ISSN:1522-1563
1522-1563
DOI:10.1152/ajpcell.00125.2012