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      Identification of Long-Lived Proteins Reveals Exceptional Stability of Essential Cellular Structures

      , , , , , ,
      Cell
      Elsevier BV

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          Abstract

          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: Copyright © 2013 Elsevier Inc. All rights reserved.

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          Author and article information

          Journal
          Cell
          Cell
          Elsevier BV
          00928674
          August 2013
          August 2013
          : 154
          : 5
          : 971-982
          Article
          10.1016/j.cell.2013.07.037
          3788602
          23993091
          355de914-758d-460b-9f24-8476d03f15fd
          © 2013

          https://www.elsevier.com/tdm/userlicense/1.0/

          https://www.elsevier.com/open-access/userlicense/1.0/

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