Interactions between autophagy receptors and ubiquitin-like proteins form the molecular basis for selective autophagy

Mol Cell. 2014 Jan 23;53(2):167-78. doi: 10.1016/j.molcel.2013.12.014.

Abstract

Selective autophagy ensures recognition and removal of various cytosolic cargoes. Hence, aggregated proteins, damaged organelles, or pathogens are enclosed into the double-membrane vesicle, the autophagosome, and delivered to the lysosome for degradation. This process is mediated by selective autophagy receptors, such as p62/SQSTM1. These proteins recognize autophagic cargo and, via binding to small ubiquitin-like modifiers (UBLs)--Atg8/LC3/GABARAPs and ATG5--mediate formation of selective autophagosomes. Recently, it was found that UBLs can directly engage the autophagosome nucleation machinery. Here, we review recent findings on selective autophagy and propose a model for selective autophagosome formation in close proximity to cargo.

Publication types

  • Review

MeSH terms

  • Autophagy / physiology*
  • Models, Biological*
  • Models, Molecular
  • Peroxisomes / metabolism
  • Signal Transduction
  • Ubiquitination
  • Ubiquitins / metabolism
  • Ubiquitins / physiology*

Substances

  • Ubiquitins