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. 2020 Nov 18;10:131. doi: 10.1186/s13578-020-00489-x

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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/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 3 — Movement and spatial distribution of lysosomes. Lysosomes can move towards the plus or minus ends of microtubules. The movement towards the plus end of microtubules is mediated by kinesins, of which the best characterized is kinesin-1, which is composed of two heavy chains (KHC) and two light chains (KLC). BORC can associate with lysosomes and recruit Arl8. SKIP binds to Arl8 through an N-terminal RUN domain and interacts with KLC through a WD motif in an unstructured region. Moreover, the ER-anchored protein protrudin binds simultaneously to Rab7 and PI3P to bridge the ER and lysosome. Protrudin then transfers lysosomes to the Rab7 effector FYCO1 and kinesin-1. The movement towards the minus end of microtubules is mediated by dynein. Lysosomal transport mediated by dynein is dependent on dynactin. The recruitment of dynein-dynactin to lysosomes is dependent on Rab7. RILP can link Rab7 to the dynactin p150-glued subunit. ORP1L forms a tripartite complex with Rab7 and RILP, promoting the association of βIII-spectrin with the dynactin Arp1 subunit. The interaction of ORP1L with Rab7–RILP and βIII-spectrin can activate dynein. The ability of ORP1L to engage is dependent on cholesterol levels. Under low-cholesterol conditions, ORP1L will bind VAPA, resulting in the dissociation of dynein-dynactin from lysosomes