Laboratory of Cardiovascular Proteomics, Centro Nacional de INvestigaciones Cardiovasculares (CNIC), CIBER de Enfermedatdes Cardiovasculares (CIBERCV), Madrid, Spain
Cells respond to environmental cues, such as external signal or stresses, by dynamically remodeling their proteome. A great part of the proteome-level regulation within a cell happens post-translationally. Post-translational regulation can involve chemical modifications in the protein, but also subcellular relocation, secretion or targeted degradation. Mass spectrometry-based proteomics offers an exceptional platform to explore from a systems-level perspective all these dynamic mechanisms. In this talk, I will present how using MS-based proteomics we can study cell response and adaptation to stress from a post-translational perspective, either by studying the spatio-temporal dynamics within the cells or their modification status.
1. P. Bortel, et al. Systematic Optimization of Automated Phosphopeptide Enrichment for High-Sensitivity Phosphoproteomics. Molecular & Cellular Proteomics 23 (2024)
2. U. H. Guzman, et al. Ultra-fast label-free quantification and comprehensive proteome coverage with narrow-window data-independent acquisition. Nat Biotechnol 42, 1855–1866 (2024)
3. A. Martínez-Val, et al. Hybrid-DIA: intelligent data acquisition integrates targeted and discovery proteomics to analyze phospho-signaling in single spheroids. Nat Commun 14, 3599 (2023).
This seminar is supported by the B2S Federation
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