Journal
CELL
Volume 154, Issue 5, Pages 971-982Publisher
CELL PRESS
DOI: 10.1016/j.cell.2013.07.037
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Funding
- Hewitt Foundation
- National Institutes of Health (NIH) [R01GM098749]
- Glenn Aging Foundation
- American Cancer Society [P30CA014195]
- Ellison Medical Foundation
- NIH [F32AG039127, P41 RR011823, P01 AG031097, R01 MH067880]
- Searle Scholars Program
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Intracellular proteins with long lifespans have recently been linked to age-dependent defects, ranging from decreased fertility to the functional decline of neurons. Why long-lived proteins exist in metabolically active cellular environments and how they are maintained over time remains poorly understood. Here, we provide a system-wide identification of proteins with exceptional lifespans in the rat brain. These proteins are inefficiently replenished despite being translated robustly throughout adulthood. Using nucleoporins as a paradigm for long-term protein persistence, we found that nuclear pore complexes (NPCs) are maintained over a cell's life through slow but finite exchange of even its most stable subcomplexes. This maintenance is limited, however, as some nucleoporin levels decrease during aging, providing a rationale for the previously observed age-dependent deterioration of NPC function. Our identification of a long-lived proteome reveals cellular components that are at increased risk for damage accumulation, linking long-term protein persistence to the cellular aging process.
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