Targeted Protein Unfolding at the Golgi Apparatus
- PMID: 36512243
- DOI: 10.1007/978-1-0716-2639-9_39
Targeted Protein Unfolding at the Golgi Apparatus
Abstract
Maintaining protein homeostasis (proteostasis) is vital to cellular and organismal health. How the Golgi apparatus, the central protein maturation and sorting station in the cell, manages misfolded proteins to maintain proteostasis is still poorly understood. Here we present a strategy for targeted protein unfolding at the Golgi that enables studying Golgi-related protein quality control and stress-signaling pathways. Targeted protein unfolding is induced by small molecule-based chemical biology approaches-hydrophobic tagging and the use of a destabilization domain. Imaging studies allow visualizing quality control (QC) phenotypes, such as the formation of QC carriers and Golgi-to-endoplasmic reticulum trafficking, and correlating these phenotypes with other trafficking processes.
Keywords: Chemical biology tools; Destabilization domain; HaloTag fusion proteins; Hydrophobic tagging; SNAP-TMR pulse labeling; Targeted protein unfolding; Trimethoprim.
© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
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