Journal article
Skeletal muscle ACC2 S212 phosphorylation is not required for the control of fatty acid oxidation during exercise
HM O’Neill, JS Lally, S Galic, T Pulinilkunnil, RJ Ford, JRB Dyck, BJ Van Denderen, BE Kemp, GR Steinberg
Physiological Reports | Published : 2015
DOI: 10.14814/phy2.12444
Open access
Abstract
During submaximal exercise fatty acids are a predominant energy source for muscle contractions. An important regulator of fatty acid oxidation is acetyl- CoA carboxylase (ACC), which exists as two isoforms (ACC1 and ACC2) with ACC2 predominating in skeletal muscle. Both ACC isoforms regulate malonyl- CoA production, an allosteric inhibitor of carnitine palmitoyltransferase 1 (CPT-1); the primary enzyme controlling fatty acyl-CoA flux into mitochondria for oxidation. AMP-activated protein kinase (AMPK) is a sensor of cellular energy status that is activated during exercise or by pharmacological agents such as metformin and AICAR. In resting muscle the activation of AMPK with AICAR leads to in..
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Funding Acknowledgements
These studies were supported by grants and fellowships from the Australian Research Council and CSIRO (BEK), National Health and Medical Research Council (BEK, GRS, BVD), the Natural Sciences and Engineering Research Council (GRS), and the Canadian Institutes of Health Research (CIHR) (GRS and JRBD). HMO supported by Australian Postgraduate Award-Melbourne University and National Health and Medical Research Council Peter Doherty Early Career Fellowship. This study was supported in part by the Victorian Government's OIS Program (BEK) and Canadian Foundation for Innovation (GRS). GRS is a Canada Research Chair in metabolism and obesity and J Bruce Duncan Chair in Metabolic Diseases.