Document Detail

AMP-activated protein kinase is required for exercise-induced peroxisome proliferator-activated receptor co-activator 1 translocation to subsarcolemmal mitochondria in skeletal muscle.
MedLine Citation:
PMID:  23297307     Owner:  NLM     Status:  MEDLINE    
In skeletal muscle, mitochondria exist as two subcellular populations known as subsarcolemmal (SS) and intermyofibrillar (IMF) mitochondria. SS mitochondria preferentially respond to exercise training, suggesting divergent transcriptional control of the mitochondrial genomes. The transcriptional co-activator peroxisome proliferator-activated receptor γ co-activator 1α (PGC-1α) and mitochondrial transcription factor A (Tfam) have been implicated in the direct regulation of the mitochondrial genome in mice, although SS and IMF differences may exist, and the potential signalling events regulating the mitochondrial content of these proteins have not been elucidated. Therefore, we examined the potential for PGC-1α and Tfam to translocate to SS and IMF mitochondria in human subjects, and performed experiments in rodents to identify signalling mechanisms regulating these translocation events. Acute exercise in humans and rats increased PGC-1α content in SS but not IMF mitochondria. Acute exposure to 5-aminoimidazole-4-carboxamide-1-β-ribofuranoside in rats recapitulated the exercise effect of increased PGC-1α protein within SS mitochondria only, suggesting that AMP-activated protein kinase (AMPK) signalling is involved. In addition, rendering AMPK inactive (AMPK kinase dead mice) prevented exercise-induced PGC-1α translocation to SS mitochondria, further suggesting that AMPK plays an integral role in these translocation events. In contrast to the conserved PGC-1α translocation to SS mitochondria across species (humans, rats and mice), acute exercise only increased mitochondrial Tfam in rats. Nevertheless, in rat resting muscle PGC-1α and Tfam co-immunoprecipate with α-tubulin, suggesting a common cytosolic localization. These data suggest that exercise causes translocation of PGC-1α preferentially to SS mitochondria in an AMPK-dependent manner.
Brennan K Smith; Kazutaka Mukai; James S Lally; Amy C Maher; Brendon J Gurd; George J F Heigenhauser; Lawrence L Spriet; Graham P Holloway
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2013-01-07
Journal Detail:
Title:  The Journal of physiology     Volume:  591     ISSN:  1469-7793     ISO Abbreviation:  J. Physiol. (Lond.)     Publication Date:  2013 Mar 
Date Detail:
Created Date:  2013-03-18     Completed Date:  2013-08-30     Revised Date:  2014-03-26    
Medline Journal Info:
Nlm Unique ID:  0266262     Medline TA:  J Physiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  1551-61     Citation Subset:  IM    
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MeSH Terms
AMP-Activated Protein Kinases / genetics,  metabolism*
Cytosol / metabolism
Heat-Shock Proteins / metabolism*
Mice, Knockout
Mitochondria, Muscle / classification,  metabolism*
Muscle, Skeletal / metabolism*,  physiology
Physical Exertion
Protein Transport
RNA-Binding Proteins / metabolism*
Rats, Sprague-Dawley
Sarcolemma / metabolism
Signal Transduction
Species Specificity
Trans-Activators / metabolism
Transcription Factors / metabolism*
Young Adult
Reg. No./Substance:
0/Heat-Shock Proteins; 0/PPARGC1A protein, human; 0/Ppargc1a protein, mouse; 0/Ppargc1a protein, rat; 0/RNA-Binding Proteins; 0/Trans-Activators; 0/Transcription Factors; EC Protein Kinases

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