Introduction: The maintenance of skeletal muscle mass and function is critical for health and wellbeing, with deterioration in muscle size and strength associated with numerous chronic diseases. Skeletal muscle protein balance is highly dependent on the activity of the serine/threonine protein kinase, mammalian target of rapamycin complex 1 (mTOR), which when active can stimulate both protein synthesis and attenuate protein degradation. Mechanism(s) of mTOR activation in human skeletal muscle after contractile activity are still not fully understood but are thought to involve signal transduction events through mechanical sensing proteins located within or in close proximity to the cell membrane. The Integrin-β proteins play a role in cardiac muscle hypertrophy; however, little is known about the role of integrin β-3 in response to resistance exercise in human skeletal muscle. Methods: Fourteen young, healthy male volunteers (24.7 ± 2.7 yrs, 177.4±6.8 cm, BMI 26.1±2.2 kg m−2) performed an acute bout of resistance exercise (4 sets of leg press and knee extension at 8-10 repetition maximum) prior to ingesting a beverage providing 20/44/1g of protein/carbohydrate/fat (PRO: n=7) to enhance post-exercise muscle anabolism or an energy-free control (CON: n=7). Muscle biopsies were collected from the vastus lateralis pre and post-exercise and 1h and 3h after beverage ingestion. Skeletal muscle samples were immediately frozen in isopentane cooled by liquid nitrogen. Samples were serially sectioned for subsequent immunofluorescent analysis. Pearson’s correlation coefficient analysis was conducted to quantify protein-membrane and protein-protein interaction. Results: Integrin β-3 was observed to translocate to the sarcolemmal membrane following resistance exercise. Quantification showed an enhanced association between Integrin β-3 and cell membrane 1 and 3h post exercise with no difference between groups (CON: 0.29±0.02 pre, 0.33±0.03 1h post, 0.31±0.03 3h post (p<0.05); PRO: 0.31±0.02 pre, 0.37±0.02 1h, 0.36±0.01 3h post (p<0.05)). In addition, we observed increased association between Integrin β-3 and mTOR on the cell periphery in both CON and PRO groups (CON: 0.40±0.02 pre, 0.44±0.03 1h, 0.45±0.03 3h post (p<0.05) and PRO: 0.43±0.02 pre, 0.49±0.02 1h, 0.48±0.02 3h post exercise respectively (p<0.05)). Conclusion: We present novel data detailing Integrin β-3 redistribution to the cell membrane following a single bout of resistance exercise. Further, we report that Integrin β-3 and mTOR interact at the cell periphery following resistance exercise, suggesting that Integrin β-3 may be involved in mTOR activation in human skeletal muscle.