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      A Role for Ubiquitin in Selective Autophagy

      , , ,
      Molecular Cell
      Elsevier BV

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          Abstract

          Ubiquitination is the hallmark of protein degradation by the 26S proteasome. However, the proteasome is limited in its capacity to degrade oligomeric and aggregated proteins. Removal of harmful protein aggregates is mediated by autophagy, a mechanism by which the cell sequesters cytosolic cargo and delivers it for degradation by the lysosome. Identification of autophagy receptors, such as p62/SQSTM1 and NBR1, which simultaneously bind both ubiquitin and autophagy-specific ubiquitin-like modifiers, LC3/GABARAP, has provided a molecular link between ubiquitination and autophagy. This review explores the hypothesis that ubiquitin represents a selective degradation signal suitable for targeting various types of cargo, ranging from protein aggregates to membrane-bound organelles and microbes.

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          Author and article information

          Journal
          Molecular Cell
          Molecular Cell
          Elsevier BV
          10972765
          May 2009
          May 2009
          : 34
          : 3
          : 259-269
          Article
          10.1016/j.molcel.2009.04.026
          19450525
          11c682e0-b8a6-419a-8821-0146a40ed214
          © 2009

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

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

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