Guest Editor
Collection Overview
Maintenance of protein homeostasis (‘proteostasis’), or the correct balance of protein synthesis, folding, localization, and degradation, is essential for cellular health. Declining proteostasis is a hallmark of aging and numerous chronic age-related diseases, such as neurodegeneration, cardiac dysfunction, and sarcopenia, among others. Conversely, enhancement of proteostasis machinery is associated with health and longevity. Therefore, quantitative measurements of protein turnover and proteostasis machinery are critical tools to assess disease mechanisms and potential therapeutic interventions.
While numerous methods exist to assess changes in proteostasis, they often rely on the measurement of markers of protein synthesis and degradation machinery as a surrogate for changes in protein turnover. With mass spectrometry-based approaches, it is possible to measure changes in protein turnover directly, quantitatively, and comprehensively across many individual proteins. Additionally, emerging molecular approaches have enabled quantitative measurement of flux through protein degradation pathways and assessment of increasingly specific degradation processes, such as aggrephagy, chaperone mediated autophagy, mitophagy, etc.
This methods collection will provide quantitative methods to measure in vivo protein turnover rates and tools to assess proteostasis machinery. These methods will include large-scale mass spectrometry-based approaches which utilize stable isotope labeling and sophisticated analysis pipelines, as well as molecular methods to quantitatively assess autophagic flux and decipher the control mechanisms underlying the clearance of proteins.
