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Am J Physiol Endocrinol Metab 290: E341-E346, 2006. First published September 27, 2005; doi:10.1152/ajpendo.00314.2005
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Exercise does not alter subcellular localization, but increases phosphorylation of insulin-signaling proteins in human skeletal muscle

Chris Wilson,1 Mark Hargreaves,1,2 and Kirsten F. Howlett1

1Center for Physical Activity and Nutrition, School of Exercise and Nutrition Sciences, Deakin University and 2Department of Physiology, The University of Melbourne, Melbourne, Australia

Submitted 12 July 2005 ; accepted in final form 20 September 2005

The subcellular localization of insulin signaling proteins is altered by various stimuli such as insulin, insulin-like growth factor I, and oxidative stress and is thought to be an important mechanism that can influence intracellular signal transduction and cellular function. This study examined the possibility that exercise may also alter the subcellular localization of insulin signaling proteins in human skeletal muscle. Nine untrained males performed 60 min of cycling exercise (~67% peak pulmonary O2 uptake). Muscle biopsies were sampled at rest, immediately after exercise, and 3 h postexercise. Muscle was fractionated by centrifugation into the following crude fractions: cytosolic, nuclear, and a high-speed pellet containing membrane and cytoskeletal components. Fractions were analyzed for protein content of insulin receptor, insulin receptor substrate (IRS)-1 and -2, p85 subunit of phosphatidylinositol 3-kinase, Akt, and glycogen synthase kinase-3 (GSK-3). There was no significant change in the protein content of the insulin signaling proteins in any of the crude fractions after exercise or 3 h postexercise. Exercise had no significant effect on the phosphorylation of IRS-1 Tyr612 in any of the fractions. In contrast, exercise increased (P < 0.05) the phosphorylation of Akt Ser473 and GSK-3{alpha}/{beta} Ser9/21 in the cytosolic fraction only. In conclusion, exercise can increase phosphorylation of downstream insulin signaling proteins specifically in the cytosolic fraction but does not result in changes in the subcellular localization of insulin signaling proteins in human skeletal muscle. Change in the subcellular protein localization is therefore an unlikely mechanism to influence signal transduction pathways and cellular function in skeletal muscle after exercise.

insulin receptor substrate; intracellular signaling pathway


Address for reprint requests and other correspondence: K. Howlett, School of Exercise and Nutrition Sciences, Deakin University, Burwood, Victoria 3125, Australia (e-mail: kirsten.howlett{at}deakin.edu.au)




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