title: Quantitative proteomics for the analysis of spatio-temporal protein dynamics during autophagy.
abstract: Stress-induced autophagy leads to major cellular remodeling. During autophagy, a new organelle, the autophagosome, is formed that shuttles cellular material to lysosomes for degradation. Quantitative mass spectrometry-based proteomics is a powerful research strategy for the description of spatio-temporal protein dynamics during autophagy. This technique allows the identification of protein-protein interactions and of specific post-translational modifications. In addition, current methods enable the in-depth characterization of cellular as well as organellar composition changes and the global analysis of signaling networks. Thus, a plastic picture of the cell can be drawn. In this review we describe recent advances in MS-based proteomics approaches and their implications for autophagy-related research questions.
authors.affiliation: Freiburg Institute for Advanced Studies (FRIAS), School of Life Sciences-LIFENET, University of Freiburg, Freiburg, Germany.
authors.forename: Andrea C
authors.initials: AC
authors.lastname: Zimmermann
authors.forename: Mostafa
authors.initials: M
authors.lastname: Zarei
authors.forename: Sven
authors.initials: S
authors.lastname: Eiselein
authors.forename: Jörn
authors.initials: J
authors.lastname: Dengjel
mesh_terms: D000818:Animals; D001343:Autophagy; D006801:Humans; D013058:Mass Spectrometry; D011485:Protein Binding; D011506:Proteins / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*; D013997:Time Factors
chemical_list: D011506:Proteins