N-terminal acetylation and replicative age affect proteasome localization and cell fitness during aging
Publication year
2015Source
Journal of Cell Science, 128, 1, (2015), pp. 109-17ISSN
Publication type
Article / Letter to editor
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Organization
Tumorimmunology
Journal title
Journal of Cell Science
Volume
vol. 128
Issue
iss. 1
Page start
p. 109
Page end
p. 17
Subject
Radboudumc 4: lnfectious Diseases and Global Health RIMLS: Radboud Institute for Molecular Life SciencesAbstract
Specific degradation of proteins is essential for virtually all cellular processes and is carried out predominantly by the proteasome. The proteasome is important for clearance of damaged cellular proteins. Damaged proteins accumulate over time and excess damaged proteins can aggregate and induce the death of old cells. In yeast, the localization of the proteasome changes dramatically during aging, possibly in response to altered proteasome activity requirements. We followed two key parameters of this process: the distribution of proteasomes in nuclear and cytosolic compartments, and the formation of cytoplasmic aggregate-like structures called proteasome storage granules (PSGs). Whereas replicative young cells efficiently relocalized proteasomes from the nucleus to the cytoplasm and formed PSGs, replicative old cells were less efficient in relocalizing the proteasome and had less PSGs. By using a microscopy-based genome-wide screen, we identified genetic factors involved in these processes. Both relocalization of the proteasome and PSG formation were affected by two of the three N-acetylation complexes. These N-acetylation complexes also had different effects on the longevity of cells, indicating that each N-acetylation complex has different roles in proteasome location and aging.
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- Academic publications [245400]
- Electronic publications [132939]
- Faculty of Medical Sciences [93207]
- Open Access publications [106460]
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