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Cited by 206Lipid metabolism and biosynthesisCellular transport and secretionAutophagy in Disease and Therapy

Spastin tethers lipid droplets to peroxisomes and directs fatty acid trafficking through ESCRT-III

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Chang, Chi-Lun, Weigel, Aubrey V., Ioannou, Maria S., Pasolli, H. Amalia, Xu, C. Shan, Peale, David R., Shtengel, Gleb, Freeman, Melanie +3 more·2019·Journal of Cell Biology
DOI 10.1083/jcb.201902061PMC PMC6683741

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Abstract

Lipid droplets (LDs) are neutral lipid storage organelles that transfer lipids to various organelles including peroxisomes. Here, we show that the hereditary spastic paraplegia protein M1 Spastin, a membrane-bound AAA ATPase found on LDs, coordinates fatty acid (FA) trafficking from LDs to peroxisomes through two interrelated mechanisms. First, M1 Spastin forms a tethering complex with peroxisomal ABCD1 to promote LD–peroxisome contact formation. Second, M1 Spastin recruits the membrane-shaping ESCRT-III proteins IST1 and CHMP1B to LDs via its MIT domain to facilitate LD-to-peroxisome FA trafficking, possibly through IST1- and CHMP1B-dependent modifications in LD membrane morphology. Furthermore, LD-to-peroxisome FA trafficking mediated by M1 Spastin is required to relieve LDs of lipid peroxidation. M1 Spastin’s dual roles in tethering LDs to peroxisomes and in recruiting ESCRT-III components to LD–peroxisome contact sites for FA trafficking may underlie the pathogenesis of diseases associated with defective FA metabolism in LDs and peroxisomes.

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  • Lipid droplet-peroxisome communication is abnormal in X-ALD adrenals.

    “Since the tethering of LDs to peroxisomes involves ABCD1 [431], it is tempting to postulate that LD–peroxisome communication is abnormal in X-ALD adrenals.”

    From Revisiting the Pathogenesis of X-Linked Adrenoleukodystrophy (2025) · cites this paper as [431]

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Cited by

Sorted by citations

Authors
Chang, C.-L., Weigel, A. V., Ioannou, M. S., Pasolli, H. A., Xu, C. S., Peale, D. R., Shtengel, G., Freeman, M., Hess, H. F., Blackstone, C., & Lippincott-Schwartz, J.
Affiliations
  • Howard Hughes Medical Institute (US)
  • National Institutes of Health (US)
  • Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA 1
ORCID
Venue
Journal of Cell Biology
Publisher
Rockefeller University Press
Published
2019-06-21
Volume
218
Issue
8
Pages
2583-2599
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
DOI
10.1083/jcb.201902061
PMC
PMC6683741
OpenAlex
W2950913191
Cited by
206
References
2
Citations by year
2026: 14 · 2025: 28 · 2024: 28 · 2023: 20 · 2022: 29 · 2021: 40 · 2020: 34 · 2019: 13
FWCI
12.11
Type
journal article
Language
en
Open access
Licence
Locations
  • The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
Funders
  • Howard Hughes Medical Institute
  • National Institute of Neurological Disorders and Stroke
  • National Institutes of Health
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Keywords
spastin, lipid droplets, peroxisomes, fatty acid trafficking, ESCRT-III, IST1, CHMP1B, MIT domain, ABCD1, AAA+ ATPase, lipid peroxidation, organelle tethering, membrane morphology, hereditary spastic paraplegia, lipid metabolism
MeSH terms
ATP Binding Cassette Transporter, Subfamily D, Member 1, Spastin, Adenosine Triphosphatases, Biological Transport, Fatty Acids, HeLa Cells, Humans, Hydrolysis, Lauric Acids, Models, Biological, Oncogene Proteins, Peroxisomes, Amino Acid Motifs, Mutant Proteins, Endosomal Sorting Complexes Required for Transport, Lipid Droplets

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