Schlotawa, Lars; Wachs, Michaela; Bernhard, Olaf; Mayer, Franz J.; Dierks, Thomas; Schmidt, Bernhard; Radhakrishnan, Karthikeyan: Recognition and ER Quality Control of Misfolded Formylglycine-Generating Enzyme by Protein Disulfide Isomerase. In: Cell Reports. Jg.24 H. 1. 2018, S. 27-37.e4
Inhalt
- Introduction
- Results
- PDI Specifically Interacts with Unstable MSD-Causing FGE Variants
- PDI Regulates Unstable and Stable FGE Variants Differentially
- The S155P Mutation Results in Non-Native Disulfide Configuration in FGE, Leading to Covalent Interaction with the PDI a’ Domain
- Covalent Interaction with PDI Is Determined by a Short Peptide Structure Resulting from Non-native Disulfide Bridging betwe ...
- Discussion
- Supplemental Information
- Acknowledgments
- References
- STAR★Methods
- Key Resources Table
- Contact for Reagent and Resource Sharing
- Experimental Model and Subject Details
- Method Details
- DNA constructs
- Cell culture and transfection
- PDI RNAi experiments
- Activity assay for sulfatases
- Coimmunoprecipitation
- Metabolic labeling and immunoprecipitation
- FGES155P-His+HisPDI complex purification
- Mass spectrometry
- Insulin-disulfide reduction assay for PDI
- Peptide binding assays
- Quantification and Statistical Analysis
- Data and Software Availability