Swapping of interaction partners with ATG5 for autophagosome maturation
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Autophagy is a tightly regulated lysosome-mediated catabolicprocess in eukaryotes that maintains cellular homeostasis. Adistinguishable feature of autophagy is the formation of double-membrane structures, autophagosome, which envelopesthe intracellular cargoes and finally degrades them by fusionwith lysosomes. So far, many structures of Atg proteins workingon the autophagosome formation have been reported,however those involved in autophagosome maturation, a fusionwith lysosome, are relatively unknown. One of the moleculesin autophagosome maturation, TECPR1, has been identifiedand recently, structural studies on both ATG5-TECPR1 andATG5-ATG16L1 complexes revealed that TECPR1 andATG16L1 share the same binding site on ATG5. These results,in combination with supporting biochemical and cellular biologicaldata, provide an insight into a model for swappingATG5 partners for autophagosome maturation.
Abstract
Autophagy is a tightly regulated lysosome-mediated catabolicprocess in eukaryotes that maintains cellular homeostasis. Adistinguishable feature of autophagy is the formation of double-membrane structures, autophagosome, which envelopesthe intracellular cargoes and finally degrades them by fusionwith lysosomes. So far, many structures of Atg proteins workingon the autophagosome formation have been reported,however those involved in autophagosome maturation, a fusionwith lysosome, are relatively unknown. One of the moleculesin autophagosome maturation, TECPR1, has been identifiedand recently, structural studies on both ATG5-TECPR1 andATG5-ATG16L1 complexes revealed that TECPR1 andATG16L1 share the same binding site on ATG5. These results,in combination with supporting biochemical and cellular biologicaldata, provide an insight into a model for swappingATG5 partners for autophagosome maturation.