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Swapping of interaction partners with ATG5 for autophagosome maturation
Swapping of interaction partners with ATG5 for autophagosome maturation
BMB Reports. 2015. Mar, 48(3): 129-130
Copyright © 2015, Korean Society for Biochemistry and Molecular Biology
This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
  • Received : March 19, 2015
  • Published : March 31, 2015
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About the Authors
Jun Hoe Kim
Hyun Kyu Song
hksong@korea.ac.kr

Abstract
Autophagy is a tightly regulated lysosome-mediated catabolic process in eukaryotes that maintains cellular homeostasis. A distinguishable feature of autophagy is the formation of double-membrane structures, autophagosome, which envelopes the intracellular cargoes and finally degrades them by fusion with lysosomes. So far, many structures of Atg proteins working on the autophagosome formation have been reported, however those involved in autophagosome maturation, a fusion with lysosome, are relatively unknown. One of the molecules in autophagosome maturation, TECPR1, has been identified and recently, structural studies on both ATG5-TECPR1 and ATG5-ATG16L1 complexes revealed that TECPR1 and ATG16L1 share the same binding site on ATG5. These results, in combination with supporting biochemical and cellular biological data, provide an insight into a model for swapping ATG5 partners for autophagosome maturation. [BMB Reports 2015; 48(3): 129-130]
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Acknowledgements
This work was supported by grants from National Research Foundation of Korea (NRF-2011-0028168 to HKS; NRF-2012-Global PhD Fellowship to JHK).
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