The AAA-ATPase p97 is essential for outer mitochondrial membrane protein turnover
Open accessAbstract
Recent studies have revealed a role for the ubiquitin/proteasome system in the regulation and turnover of outer mitochondrial membrane (OMM)-associated proteins. Although several molecular components required for this process have been identified, the mechanism of proteasome-dependent degradation of OMM-associated proteins is currently unclear. We show that an AAA-ATPase, p97, is required for the proteasomal degradation of Mcl1 and Mfn1, two unrelated OMM proteins with short half-lives. A number of biochemical assays, as well as imaging of changes in localization of photoactivable GFP-fused Mcl1, revealed that p97 regulates the retrotranslocation of Mcl1 from mitochondria to the cytosol, prior to, or concurrent with, proteasomal degradation. Mcl1 retrotranslocation from the OMM depends on the activity of the ATPase domain of p97. Furthermore, p97-mediated retrotranslocation of Mcl1 can be recapitulated in vitro, confirming a direct mitochondrial role for p97. Our results establish p97 as a novel and essential component of the OMM-associated protein degradation pathway.
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p97 provides the driving force to extract Mfn1, Mfn2, and MCL1 from the OMM and chaperone them to the proteasome.
“p97 provides the driving force to extract Mfn1, Mfn2, and the anti-apoptotic protein MCL1 from the OMM and chaperone them to the proteasome [49, 50].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [50]
p97/VCP is critical in the retrotranslocation and degradation of endoplasmic reticulum-associated proteins (ERAD) and mitochondrial proteins (MAD).
“p97/VCP is critical in the retrotranslocation and degradation of endoplasmic reticulum-associated proteins (ERAD) [47] and mitochondrial proteins ( MAD) [49, 50].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [50]
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Self-citation
- Authors
- Xu, S., Peng, G., Wang, Y., Fang, S., & Karbowski, M.
- Affiliations
- University of Maryland, Baltimore (US)
- Corresponding author
- Karbowski, Mariusz
- Venue
- Molecular Biology of the Cell
- Published
- 2011-02
- Volume
- 22
- Issue
- 3
- Pages
- 291-300
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- PMC
- PMC3031461
- OpenAlex
- W2082069715
- Cited by
- 243
- References
- 46
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 12 · 2023: 14 · 2022: 12 · 2021: 16 · 2020: 21 · 2019: 16 · 2018: 17 · 2017: 15 · 2016: 23 · 2015: 15 · 2014: 23 · 2013: 19 · 2012: 16
- FWCI
- 6.26
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- Molecular Biology of the Cell (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM083131)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- VCP, AAA+ ATPase, mitochondrial outer membrane, protein turnover, proteasomal degradation, Mcl-1, Mfn1, retrotranslocation, ubiquitin-proteasome system, mitochondrial protein degradation, ATPase domain
- MeSH terms
- Adenosine Triphosphatases, Cytosol, HeLa Cells, Humans, Nuclear Proteins, Recombinant Fusion Proteins, Protein Structure, Tertiary, Proto-Oncogene Proteins c-bcl-2, GTP Phosphohydrolases, Protein Transport, Mitochondrial Proteins, Membrane Transport Proteins, Mitochondrial Membrane Transport Proteins, Proteasome Endopeptidase Complex, Green Fluorescent Proteins, Mitochondrial Membranes, Protein Stability, Myeloid Cell Leukemia Sequence 1 Protein
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