| Autor: |
Navarrete-Perea J; Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02155, United States., Guerra-Moreno A; Brigham and Women's Hospital, Boston, Massachusetts 02115, United States., Van Vranken J; Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02155, United States., Isasa M; C4 Therapeutics, Cambridge, Massachusetts 02142, United States., Paulo JA; Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02155, United States., Gygi SP; Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02155, United States. |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of proteome research [J Proteome Res] 2021 May 07; Vol. 20 (5), pp. 2751-2761. Date of Electronic Publication: 2021 Apr 02. |
| DOI: |
10.1021/acs.jproteome.1c00035 |
| Abstrakt: |
Iron is an essential element for life, as it is critical for oxygen transport, cellular respiration, DNA synthesis, and metabolism. Disruptions in iron metabolism have been associated with several complex diseases like diabetes, cancer, infection susceptibility, neurodegeneration, and others; however, the molecular mechanisms linking iron metabolism with these diseases are not fully understood. A commonly used model to study iron deficiency (ID) is yeast, Saccharomyces cerevisiae . Here, we used quantitative (phospho)proteomics to explore the early (4 and 6 h) and late (12 h) response to ID. We showed that metabolic pathways like the Krebs cycle, amino acid, and ergosterol biosynthesis were affected by ID. In addition, during the late response, several proteins related to the ubiquitin-proteasome system and autophagy were upregulated. We also explored the proteomic changes during a recovery period after 12 h of ID. Several proteins recovered their steady-state levels, but some others, such as cytochromes, did not recover during the time tested. Additionally, we showed that autophagy is active during ID, and some of the degraded proteins during ID can be rescued using KO strains for several key autophagy genes. Our results highlight the complex proteome changes occurring during ID and recovery. This study constitutes a valuable data set for researchers interested in iron biology, offering a temporal proteomic data set for ID, as well as a compendium the proteomic changes associated with episodes of iron recovery. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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