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. 2020 Nov 5;12(7):520–544. doi: 10.1007/s13238-020-00793-9

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© The Author(s) 2020

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Model for SNARE-mediated autophagosome-lysosome fusion. Autophagosome-lysosome fusion is the key step of autophagy and is highly regulated by SNARE proteins, tethering factors, Rab GTPase, SM proteins, and other proteins. The fusion SNAREs identified so far for autophagy include STX17-SNAP29-VAMP8 and YKT6/SNAP29/STX7. Sealed autophagosome recruits the SNARE binary complex together with lysosomal SNARE protein to form a four-helix bundle to mediate autophagosome-lysosome fusion. Besides, tethering between autophagosomes and lysosomes can promote this fusion. Proteins involved in tethering include ATG14, Rab GTPase, HOPS, PLEKHM1, UVRAG, EPG5, BRUCE, TECPR1, GRASP55, etc