Interactions between autophagy receptors and ubiquitin-like proteins form the molecular basis for selective autophagy.
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.
Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Marie Curie Strasse 9, 60439 Frankfurt am Main, Germany.
Vladimir
V
Rogov
Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Marie Curie Strasse 9, 60439 Frankfurt am Main, Germany.
Volker
V
Dötsch
Molecular Cancer Research Group, Institute of Medical Biology, University of Tromsø, 9037 Tromsø, Norway.
Terje
T
Johansen
Merck KGaA, Frankfurter Strasse 250, 64293 Darmstadt, Germany. Electronic address: vladimir.kirkin@merckgroup.com.
Vladimir
V
Kirkin
D001343:Autophagy / Q000502:physiology*; D008954:Models, Biological; D008958:Models, Molecular; D020675:Peroxisomes / Q000378:metabolism; D015398:Signal Transduction; D054875:Ubiquitination; D014452:Ubiquitins / Q000378:metabolism / Q000502:physiology*
D014452:Ubiquitins