title: Proteome dynamics: revisiting turnover with a global perspective.
abstract: Although bulk protein turnover has been measured with the use of stable isotope labeled tracers for over half a century, it is only recently that the same approach has become applicable to the level of the proteome, permitting analysis of the turnover of many proteins instead of single proteins or an aggregated protein pool. The optimal experimental design for turnover studies is dependent on the nature of the biological system under study, which dictates the choice of precursor label, protein pool sampling strategy, and treatment of data. In this review we discuss different approaches and, in particular, explore how complexity in experimental design and data processing increases as we shift from unicellular to multicellular systems, in particular animals.
authors.affiliation: Protein Function Group, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, United Kingdom.
authors.forename: Amy J
authors.initials: AJ
authors.lastname: Claydon
authors.forename: Robert
authors.initials: R
authors.lastname: Beynon
mesh_terms: D000818:Animals; D006801:Humans; D007553:Isotope Labeling; D011506:Proteins / Q000032:analysis* / Q000378:metabolism; D059748:Proteolysis; D020543:Proteome / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*; D013194:Staining and Labeling
chemical_list: D011506:Proteins; D020543:Proteome