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A molecular mechanism to regulate lysosome motility for lysosome positioning and tubulation
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To mediate the degradation of biomacromolecules, lysosomes must traffic towards cargo-carrying vesicles for subsequent membrane fusion or fission. Mutations of the lysosomal Ca(2+) channel TRPML1 cause lysosomal storage disease (LSD) characterized by disordered lysosomal membrane trafficking in cells. Here we show that TRPML1 activity is required to promote Ca(2+)-dependent centripetal movement of lysosomes towards the perinuclear region (where autophagosomes accumulate) following autophagy induction. ALG-2, an EF-hand-containing protein, serves as a lysosomal Ca(2+) sensor that associates physically with the minus-end-directed dynactin-dynein motor, while PtdIns(3,5)P(2), a lysosome-localized phosphoinositide, acts upstream of TRPML1. Furthermore, the PtdIns(3,5)P(2)-TRPML1-ALG-2-dynein signalling is necessary for lysosome tubulation and reformation. In contrast, the TRPML1 pathway is not required for the perinuclear accumulation of lysosomes observed in many LSDs, which is instead likely to be caused by secondary cholesterol accumulation that constitutively activates Rab7-RILP-dependent retrograde transport. Ca(2+) release from lysosomes thus provides an on-demand mechanism regulating lysosome motility, positioning and tubulation.
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“This may be explained by recent observations showing that JIP4 phosphorylation following oxidative stress induces its interaction with the TRPML1/ALG2 complex, which also mediates dynein-dependent retrograde transport of lysosomes9,38,39.”
From TMEM55B links autophagy flux, lysosomal repair, and TFE3 activation in response to oxidative stress (2024) · cites this paper as [39]
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“ALG-2 interacts with the lysosomal transient receptor potential channel MCOLN1 in a calcium-dependent manner to recruit dynein–dynactin to lysosomes28,29.”
From TFEB regulates lysosomal positioning by modulating TMEM55B expression and JIP4 recruitment to lysosomes (2017) · cites this paper as [28]
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“a phenotype previously observed in association with lysosomal impairment41,42”
From Decreased lipidated ApoE‐receptor interactions confer protection against pathogenicity of ApoE and its lipid cargoes in lysosomes (2025) · cites this paper as [42]
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Self-citation
Metadata
- Authors
- Li, X., Rydzewski, N., Hider, A., Zhang, X., Yang, J., Wang, W., Gao, Q., Cheng, X., & Xu, H.
- Affiliations
- University of Michigan (US)
- Zhejiang University of Technology (CN)
- Corresponding author
- Xu, Haoxing
- ORCID
- Venue
- Nature Cell Biology
- Published
- 2016-03-07
- Volume
- 18
- Issue
- 4
- Pages
- 404-417
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC4871318
- OpenAlex
- W2299614729
- Cited by
- 387
- References
- 146
- Citations by year
- 2026: 26 · 2025: 25 · 2024: 38 · 2023: 36 · 2022: 46 · 2021: 44 · 2020: 42 · 2019: 30 · 2018: 44 · 2017: 39 · 2016: 17
- FWCI
- 39.52
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Deep Blue (University of Michigan) (submittedVersion)
- Funders
- National Institute of Mental Health (MH096595, R03MH096595)
- National Institute of Neurological Disorders and Stroke (R21NS091928, NS062792, R01NS062792)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR060837, R01AR060837)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- lysosome motility, lysosome positioning, TRPML1, lysosomal storage disease, ALG-2, PtdIns(3,5)P2, autophagy, lysosomal calcium release, retrograde transport, cholesterol accumulation, perinuclear accumulation
- MeSH terms
- rab7 GTP-Binding Proteins, Animals, Autophagy, Base Sequence, Calcium, Calcium-Binding Proteins, Cell Line, Chlorocebus aethiops, Dyneins, HeLa Cells, Humans, Luminescent Proteins, Lysosomes, Microscopy, Fluorescence, Models, Biological, Molecular Sequence Data, Mutation, Signal Transduction, Phosphatidylinositol Phosphates, Mice, Knockout, COS Cells, rab GTP-Binding Proteins, Fluorescence Recovery After Photobleaching, Adaptor Proteins, Signal Transducing, Transient Receptor Potential Channels, Apoptosis Regulatory Proteins, HEK293 Cells
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