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Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics
Published on: June 23, 2022
Organelle proteomics by label-free and SILAC-based protein correlation profiling
Joern Dengjel1, Lis Jakobsen, Jens S Andersen
1Center for Experimental BioInformatics, Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark.
Methods in Molecular Biology (Clifton, N.J.)
|September 15, 2010
Summary
Identifying true organelle proteins from contaminants is challenging. New methods using protein correlation profiling and quantitative mass spectrometry help create accurate organelle inventories for future research.
Area of Science:
- Cell Biology
- Proteomics
Background:
- Large-scale purification of cell organelles and protein complexes, coupled with mass spectrometry, yields extensive data on protein localization and function.
- A significant hurdle is distinguishing genuine organelle components from co-purifying contaminants due to imperfect biochemical purification methods.
Purpose of the Study:
- To address the challenge of identifying bona fide organelle components.
- To develop alternative strategies for analyzing organelle composition using existing data.
Main Methods:
- Utilizing information from the fractionation profiles of organelles isolated by density gradient centrifugation.
- Employing protein correlation profiling and quantitative mass spectrometry to identify candidate proteins.
Main Results:
- Development of strategies to differentiate true organelle proteins from contaminants.
- Creation of organelle inventories based on integrated proteomic and fractionation data.
Conclusions:
- The developed methods provide a robust framework for identifying organelle components.
- The defined organelle inventories are valuable for guiding subsequent functional studies in cell biology.
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