Kim, Jun Hoe Hong, Seung Beom Lee, Jae Keun Han, Sisu Roh, Kyung-Hye Lee, Kyung-Eun Kim, Yoon Ki Choi, Eui-Ju Song, Hyun Kyu 2024-01-20T08:02:20Z 2024-01-20T08:02:20Z 2021-09-05 2015-01 1554-8627 https://pubs.kist.re.kr/handle/201004/125913 Autophagy is a bulky catabolic process that responds to nutrient homeostasis and extracellular stress signals and is a conserved mechanism in all eukaryotes. When autophagy is induced, cellular components are sequestered within an autophagosome and finally degraded by subsequent fusion with a lysosome. During this process, the ATG12-ATG5 conjugate requires 2 different binding partners, ATG16L1 for autophagosome elongation and TECPR1 for lysosomal fusion. In our current study, we describe the crystal structures of human ATG5 in complex with an N-terminal domain of ATG16L1 as well as an internal AIR domain of TECPR1. Both binding partners exhibit a similar a-helical structure containing a conserved binding motif termed AFIM. Furthermore, we characterize the critical role of the C-terminal unstructured region of the AIR domain of TECPR1. These findings are further confirmed by biochemical and cell biological analyses. These results provide new insights into the molecular details of the autophagosome maturation process, from its elongation to its fusion with a lysosome. English TAYLOR & FRANCIS INC ATG12-ATG5 CONJUGATE INFLUENZA HEMAGGLUTININ SELECTIVE AUTOPHAGY LC3 LIPIDATION MEMBRANE PROTEIN MECHANISM UBIQUITIN COMPLEX TARGETS Insights into autophagosome maturation revealed by the structures of ATG5 with its interacting partners Article 10.4161/15548627.2014.984276 1 AUTOPHAGY, v.11, no.1, pp.75 - 87 AUTOPHAGY 11 1 75 87 scie scopus 000352773700006 2-s2.0-84923329832 Cell Biology Cell Biology Article ATG12-ATG5 CONJUGATE INFLUENZA HEMAGGLUTININ SELECTIVE AUTOPHAGY LC3 LIPIDATION MEMBRANE PROTEIN MECHANISM UBIQUITIN COMPLEX TARGETS autophagy ATG5 ATG12 ATG16 crystal structure lysosome fusion TECPR1