Simultaneous proteome localization and turnover analysis reveals spatiotemporal features of protein homeostasis disruptions.

ABSTRACT: The functions of proteins depend on their spatial and temporal distributions, which are not directly measured by static protein abundance. Under endoplasmic reticulum (ER) stress, the unfolded protein response (UPR) pathway remediates proteostasis in part by altering the turnover kinetics and spatial distribution of proteins. A global view of these spatiotemporal changes has yet to emerge and it is unknown how they affect different cellular compartments and pathways. Here we describe a mass spectrometry-based proteomics strategy and data analysis pipeline, termed Simultaneous Proteome Localization and Turnover (SPLAT), to measure concurrently the changes in protein turnover and subcellular distribution in the same experiment. Investigating two common UPR models of thapsigargin and tunicamy

SUBMITTER: Currie J 

PROVIDER: S-EPMC9881985 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature