Abstract
Adaptor protein complex 5 (AP-5) and its partners, SPG11 and SPG15, are recruited onto late endosomes and lysosomes. Here we show that recruitment of AP-5/SPG11/SPG15 is enhanced in starved cells and occurs by coincidence detection, requiring both phosphatidylinositol 3-phosphate (PI3P) and Rag GTPases. PI3P binding is via the SPG15 FYVE domain, which, on its own, localizes to early endosomes. GDP-locked RagC promotes recruitment of AP-5/SPG11/SPG15, while GTP-locked RagA prevents its recruitment. Our results uncover an interplay between AP-5/SPG11/SPG15 and the mTORC1 pathway and help to explain the phenotype of AP-5/SPG11/SPG15 deficiency in patients, including the defect in autophagic lysosome reformation.
© 2021 Hirst et al.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Vesicular Transport / metabolism*
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Carrier Proteins / chemistry
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Carrier Proteins / metabolism*
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Endosomes / metabolism
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HEK293 Cells
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HeLa Cells
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Humans
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Lysosomes / metabolism
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Mechanistic Target of Rapamycin Complex 1 / metabolism
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Models, Biological
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Monomeric GTP-Binding Proteins / metabolism*
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Multiprotein Complexes / metabolism*
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Nucleotides / metabolism
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Phosphatidylinositol 3-Kinases / metabolism
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Phosphatidylinositol Phosphates / metabolism*
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Protein Domains
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Proteins / metabolism*
Substances
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Adaptor Proteins, Vesicular Transport
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Carrier Proteins
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Multiprotein Complexes
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Nucleotides
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Phosphatidylinositol Phosphates
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Proteins
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SPG11 protein, human
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ZFYVE26 protein, human
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phosphatidylinositol 3-phosphate
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PIKFYVE protein, human
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Mechanistic Target of Rapamycin Complex 1
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Monomeric GTP-Binding Proteins