CALL FOR PAPERS Proteomic and Metabolomic Approaches to Cell Physiology and Pathophysiology Understanding the acetylome: translating targeted proteomics into meaningful physiology

Philp A, Rowland T, Perez-Schindler J, Schenk S. Understanding the acetylome: translating targeted proteomics into meaningful physiology. Am J Physiol Cell Physiol 307: C763–C773, 2014. First published September 3, 2014; doi:10.1152/ajpcell.00399.2013.—It is well established that exercise elicits a finely tuned adaptive response in skeletal muscle, with contraction frequency, duration, and recovery shaping skeletal muscle plasticity. Given the power of physical activity to regulate metabolic health, numerous research groups have focused on the molecular mechanisms that sense, interpret, and translate this contractile signal into postexercise adaptation. While our current understanding is that contraction-sensitive allosteric factors (e.g., Ca , AMP, NAD , and acetylCoA) initiate signaling changes, how the muscle translates changes in these factors into the appropriate adaptive response remains poorly understood. During the past decade, systems biology approaches, utilizing “omics” screening techniques, have allowed researchers to define global processes of regulation with incredible sensitivity and specificity. As a result, physiologists are now able to study substrate flux with stable isotope tracers in combination with metabolomic approaches and to coordinate these functional changes with proteomic and transcriptomic analysis. In this review, we highlight lysine acetylation as an important posttranslational modification in skeletal muscle. We discuss the evolution of acetylation research and detail how large proteomic screens in diverse metabolic systems have led to the current hypothesis that acetylation may be a fundamental mechanism to fine-tune metabolic adaptation in skeletal muscle.