Subcellular mass spectrometry reveals proteome remodeling in an asymmetrically dividing (frog) embryonic stem cell
Abstract
Subcellular proteomics maps protein localization within restricted domains of a cell, complementing high-resolution imaging by expanding the number of proteins that can be profiled at once. Achieving this at depth from subcellular inputs remains challenging. Here, we advance microprobe capillary electrophoresis–mass spectrometry (CE–MS) with trapped ion mobility spectrometry and data-independent acquisition (diaPASEF) to quantify more than a thousand proteins from opposite poles of an asymmetrically dividing embryonic blastomere in live Xenopus laevis embryos. From ~200 pg of HeLa digest—approximately 80% of a cell—the technology identified 1,035 proteins with high reproducibility in quantification (coefficient of variation
Fields of Study & Subjects
Advanced Proteomics Techniques and Applications
Mass Spectrometry Techniques and Applications
Biotin and Related Studies
Publication details
- Journal / source
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Volume
- 123
- Issue
- 5
- Pages
- e2518372123–e2518372123
- Publication date
- 26 January 2026
- Language
- EN