Identification of Long-Lived Proteins Reveals Exceptional Stability of Essential Cellular Structures
In: Cell, Jg. 154 (2013-08-01), Heft 5
Online
academicJournal
- 971 - 982
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. PAPERCLIP:
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Identification of Long-Lived Proteins Reveals Exceptional Stability of Essential Cellular Structures
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Autor/in / Beteiligte Person: | Toyama, Brandon H ; Savas, Jeffrey N ; Park, Sung Kyu ; Harris, Michael S ; Ingolia, Nicholas T ; Yates, John R ; Hetzer, Martin W |
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Zeitschrift: | Cell, Jg. 154 (2013-08-01), Heft 5 |
Veröffentlichung: | eScholarship, University of California, 2013 |
Medientyp: | academicJournal |
Umfang: | 971 - 982 |
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