A role for ubiquitin in selective autophagy

Mol Cell. 2009 May 15;34(3):259-69. doi: 10.1016/j.molcel.2009.04.026.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adaptor Proteins, Signal Transducing / metabolism
  • Autophagy / physiology*
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism
  • Histone Deacetylase 6
  • Histone Deacetylases / metabolism
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Mitochondria / metabolism
  • Peroxisomes / metabolism
  • Phagosomes / metabolism
  • Proteasome Endopeptidase Complex / metabolism
  • Protein Transport
  • Proteins / metabolism
  • Ribosomes / metabolism
  • Ubiquitin / metabolism*
  • Ubiquitination


  • Adaptor Proteins, Signal Transducing
  • Fungal Proteins
  • Intracellular Signaling Peptides and Proteins
  • NBR1 protein, human
  • Proteins
  • Ubiquitin
  • Proteasome Endopeptidase Complex
  • HDAC6 protein, human
  • Histone Deacetylase 6
  • Histone Deacetylases