Home > Publications database > P53-dependent hypusination of eIF5A affects mitochondrial translation and senescence immune surveillance. > print

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024 7 _ |a 10.1038/s41467-024-51901-w
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100 1 _ |a Jiang, Xiangli
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245 _ _ |a P53-dependent hypusination of eIF5A affects mitochondrial translation and senescence immune surveillance.
260 _ _ |a [London]
|c 2024
|b Nature Publishing Group UK
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520 _ _ |a Cellular senescence is characterized by a permanent growth arrest and is associated with tissue aging and cancer. Senescent cells secrete a number of different cytokines referred to as the senescence-associated secretory phenotype (SASP), which impacts the surrounding tissue and immune response. Here, we find that senescent cells exhibit higher rates of protein synthesis compared to proliferating cells and identify eIF5A as a crucial regulator of this process. Polyamine metabolism and hypusination of eIF5A play a pivotal role in sustaining elevated levels of protein synthesis in senescent cells. Mechanistically, we identify a p53-dependent program in senescent cells that maintains hypusination levels of eIF5A. Finally, we demonstrate that functional eIF5A is required for synthesizing mitochondrial ribosomal proteins and monitoring the immune clearance of premalignant senescent cells in vivo. Our findings establish an important role of protein synthesis during cellular senescence and suggest a link between eIF5A, polyamine metabolism, and senescence immune surveillance.
536 _ _ |a 312 - Funktionelle und strukturelle Genomforschung (POF4-312)
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650 _ 7 |a Peptide Initiation Factors
|2 NLM Chemicals
650 _ 7 |a Eukaryotic Translation Initiation Factor 5A
|2 NLM Chemicals
650 _ 7 |a Tumor Suppressor Protein p53
|2 NLM Chemicals
650 _ 7 |a RNA-Binding Proteins
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650 _ 7 |a Polyamines
|2 NLM Chemicals
650 _ 7 |a Ribosomal Proteins
|2 NLM Chemicals
650 _ 7 |a hypusine
|0 3874VXF092
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650 _ 7 |a Lysine
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650 _ 2 |a Peptide Initiation Factors: metabolism
|2 MeSH
650 _ 2 |a Peptide Initiation Factors: genetics
|2 MeSH
650 _ 2 |a Eukaryotic Translation Initiation Factor 5A
|2 MeSH
650 _ 2 |a Cellular Senescence
|2 MeSH
650 _ 2 |a Tumor Suppressor Protein p53: metabolism
|2 MeSH
650 _ 2 |a RNA-Binding Proteins: metabolism
|2 MeSH
650 _ 2 |a RNA-Binding Proteins: genetics
|2 MeSH
650 _ 2 |a Humans
|2 MeSH
650 _ 2 |a Protein Biosynthesis
|2 MeSH
650 _ 2 |a Mitochondria: metabolism
|2 MeSH
650 _ 2 |a Animals
|2 MeSH
650 _ 2 |a Mice
|2 MeSH
650 _ 2 |a Immunologic Surveillance
|2 MeSH
650 _ 2 |a Polyamines: metabolism
|2 MeSH
650 _ 2 |a Ribosomal Proteins: metabolism
|2 MeSH
650 _ 2 |a Ribosomal Proteins: genetics
|2 MeSH
650 _ 2 |a Lysine: metabolism
|2 MeSH
650 _ 2 |a Lysine: analogs & derivatives
|2 MeSH
700 1 _ |a Baig, Ali Hyder
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700 1 _ |a Palazzo, Giuliana
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700 1 _ |a Del Pizzo, Rossella
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700 1 _ |a Bortecen, Toman
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700 1 _ |a Groessl, Sven
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700 1 _ |a Zaal, Esther A
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700 1 _ |a Amaya Ramirez, Cinthia Claudia
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700 1 _ |a Kowar, Alexander
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700 1 _ |a Aviles-Huerta, Daniela
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700 1 _ |a Berkers, Celia R
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700 1 _ |a Palm, Wilhelm
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700 1 _ |a Krijgsveld, Jeroen
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700 1 _ |a Loayza-Puch, Fabricio
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773 _ _ |a 10.1038/s41467-024-51901-w
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