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Global and Site-Specific Effect of Phosphorylation on Protein Turnover
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SYSNO ASEP 0539825 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Global and Site-Specific Effect of Phosphorylation on Protein Turnover Author(s) Wu, C. (US)
Ba, Q. (US)
Lü, D. (CN)
Li, W. (US)
Šalovská, Barbora (UMG-J)
Hou, P. (US)
Mueller, T. (DE)
Rosenberger, G. (US)
Gao, E. (US)
Di, Y. (US)
Zhou, H. (CN)
Fornasiero, E.F. (DE)
Liu, Y. (US)Number of authors 13 Source Title Developmental Cell. - : Cell Press - ISSN 1534-5807
Roč. 56, č. 1 (2021), s. 111-124Number of pages 14 s. Publication form Online - E Language eng - English Country US - United States Keywords data-independent acquisition ; cell-culture ; dynamics ; quantification ; identification ; proteomics ; stability ; reveals ; peptide ; silac Subject RIV EB - Genetics ; Molecular Biology OECD category Cell biology Method of publishing Limited access Institutional support UMG-J - RVO:68378050 UT WOS 000607158400011 DOI 10.1016/j.devcel.2020.10.025 Annotation To date, the effects of specific modification types and sites on protein lifetime have not been systematically illustrated. Here, we describe a proteomic method, DeltaSILAC, to quantitatively assess the impact of site-specific phosphorylation on the turnover of thousands of proteins in live cells. Based on the accurate and reproducible mass spectrometry-based method, a pulse labeling approach using stable isotope-labeled amino acids in cells (pSILAC), phosphoproteomics, and a unique peptide-level matching strategy, our DeltaSILAC profiling revealed a global, unexpected delaying effect of many phosphosites on protein turnover. We further found that phosphorylated sites accelerating protein turnover are functionally selected for cell fitness, enriched in Cyclin-dependent kinase substrates, and evolutionarily conserved, whereas the glutamic acids surrounding phosphosites significantly delay protein turnover. Our method represents a generalizable approach and provides a rich resource for prioritizing the effects of phosphorylation sites on protein lifetime in the context of cell signaling and disease biology. Workplace Institute of Molecular Genetics Contact Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Year of Publishing 2022 Electronic address https://www.cell.com/developmental-cell/fulltext/S1534-5807(20)30875-3?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS1534580720308753%3Fshowall%3Dtrue
Number of the records: 1