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. 2022 Feb 8;13(2):132. doi: 10.1038/s41419-022-04593-3

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© The Author(s) 2022

Open Access This 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — a Chaperone-mediated autophagy degrades the LD coat proteins perilipin 2 and perilipin 3 through the coordinated action of heat-shock cognate 71 kDa protein (HSC70) and receptor lysosome-associated membrane glycoprotein 2A (LAMP2A). b Degradation of the LD coat proteins PLP2 and PLP3 allows lipase- and fat-soluble organelles to enter and undergo lipolysis. c Lipophagy induces engulfment of small cytoplasmic lipid droplets or large cytoplasmic lipid droplets by LC3-II-positive membranes. Lipid droplets are transported to lysosomes and degraded by lysosomal acid lipase (LAL). Rab7 promotes the decomposition of LDs by interacting with its downstream effector RILP. The fatty acids produced are mainly directed to the mitochondria to participate in the β-oxidation pathway.