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

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

Author information

1
Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Marie Curie Strasse 9, 60439 Frankfurt am Main, Germany.
2
Molecular Cancer Research Group, Institute of Medical Biology, University of Tromsø, 9037 Tromsø, Norway.
3
Merck KGaA, Frankfurter Strasse 250, 64293 Darmstadt, Germany. Electronic address: vladimir.kirkin@merckgroup.com.

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.

PMID:
24462201
DOI:
10.1016/j.molcel.2013.12.014
[Indexed for MEDLINE]
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