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VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD
Open accessAbstract
VCP (VCP/p97) is a ubiquitously expressed member of the AAA(+)-ATPase family of chaperone-like proteins that regulates numerous cellular processes including chromatin decondensation, homotypic membrane fusion and ubiquitin-dependent protein degradation by the proteasome. Mutations in VCP cause a multisystem degenerative disease consisting of inclusion body myopathy, Paget disease of bone, and frontotemporal dementia (IBMPFD). Here we show that VCP is essential for autophagosome maturation. We generated cells stably expressing dual-tagged LC3 (mCherry-EGFP-LC3) which permit monitoring of autophagosome maturation. We determined that VCP deficiency by RNAi-mediated knockdown or overexpression of dominant-negative VCP results in significant accumulation of immature autophagic vesicles, some of which are abnormally large, acidified and exhibit cathepsin B activity. Furthermore, expression of disease-associated VCP mutants (R155H and A232E) also causes this autophagy defect. VCP was found to be essential to autophagosome maturation under basal conditions and in cells challenged by proteasome inhibition, but not in cells challenged by starvation, suggesting that VCP might be selectively required for autophagic degradation of ubiquitinated substrates. Indeed, a high percentage of the accumulated autophagic vesicles contain ubiquitin-positive contents, a feature that is not observed in autophagic vesicles that accumulate following starvation or treatment with Bafilomycin A. Finally, we show accumulation of numerous, large LAMP-1 and LAMP-2-positive vacuoles and accumulation of LC3-II in myoblasts derived from patients with IBMPFD. We conclude that VCP is essential for maturation of ubiquitin-containing autophagosomes and that defect in this function may contribute to IBMPFD pathogenesis.
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“suggesting a late-stage block in the fusion of lysosomes with autophagosomes [249].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [249]
In the citing paper
“muscle from IBMPFD patients carrying VCP mutations [246] and transgenic mice expressing VCP mutants [244,248,249] display accumulations of SQSTM1- and LC3-positive autophagosomes and abnormal mitochondria [250,251].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [249]
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“enlarged and acidified autophagic vacuoles accumulate in cells expressing disease-associated VCP mutants, suggesting a late-stage block in the fusion of lysosomes with autophagosomes [249].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [249]
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“In IBMPFD murine muscle lysates, VCP mutations disrupt autophagosome maturation and fusion with lysosomes, but not the formation of early autophagosome precursors [246,249].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [249]
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Metadata
- Authors
- Tresse, E., Salomons, F. A., Vesa, J., Bott, L. C., Kimonis, V., Yao, T.-P., Dantuma, N. P., & Taylor, J. P.
- Affiliations
- St. Jude Children's Research Hospital (US)
- Karolinska Institutet (SE)
- University of California, Irvine (US)
- Corresponding author
- Taylor, J. Paul
- ORCID
- Venue
- Autophagy
- Publisher
- Informa UK Limited
- Published
- 2010-02-16
- Volume
- 6
- Issue
- 2
- Pages
- 217-227
- ISSN
- 1554-8627 (ISSN-L)
- 1554-8635
- PMC
- PMC2929010
- OpenAlex
- W2139772062
- Cited by
- 437
- References
- 38
- Citations by year
- 2026: 6 · 2025: 15 · 2024: 24 · 2023: 15 · 2022: 23 · 2021: 31 · 2020: 24 · 2019: 20 · 2018: 25 · 2017: 29 · 2016: 40 · 2015: 27 · 2014: 30 · 2013: 40 · 2012: 36
- FWCI
- 29.88
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc
- Locations
- Autophagy (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- DukeSpace (Duke University) (submittedVersion, cc-by-nc-nd)
- eScholarship (California Digital Library) (submittedVersion, cc-by)
- Funders
- Dana Foundation
- Karolinska Institutet
- National Institutes of Health
- National Institute on Aging (R01AG031587, AG031587)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Keywords
- VCP/p97, AAA+ ATPase, autophagosome maturation, LC3, LAMP1, LAMP2, proteasome inhibition, myoblasts
- MeSH terms
- Valosin Containing Protein, Adenosine Triphosphatases, Animals, Cathepsin B, Cells, Cultured, Humans, Microtubule-Associated Proteins, Mutation, Osteitis Deformans, Phagosomes, Recombinant Fusion Proteins, Syndrome, Vacuoles, Cell Cycle Proteins, Myositis, Inclusion Body, Ubiquitin, Myoblasts, RNA Interference, Proteasome Endopeptidase Complex, Mice, Lysosomal-Associated Membrane Protein 1, Lysosomal-Associated Membrane Protein 2, Frontotemporal Dementia
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