ZFAND5/ZNF216 is an activator of the 26S proteasome that stimulates overall protein degradation
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Significance: ZFAND5/ZNF216, a member of the ubiquitous ZFAND protein family, contains two zinc finger domains. It is induced in skeletal muscle during atrophy and was shown to be essential for the resulting large loss of muscle mass. We show here that purified ZFAND5 stimulates the 26S proteasomes’ capacity to degrade peptides and ubiquitinated proteins. In cells, it promotes the degradation of endogenous cell proteins through its ubiquitin-binding zinc finger domain (A20). Unlike several ZFAND proteins, it is not induced in proteotoxic stresses. Unlike other proteasome activators, ZFAND5 actually stimulates overall protein breakdown by the ubiquitin proteasome pathway.
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ZNF216 binds the 26S proteasome and enhances proteolytic activity by increasing ATP hydrolysis.
“The zinc finger protein ZNF216 binds the 26S proteasome and enhances the proteolytic activity by increasing ATP hydrolysis58.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [58]
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References 47 · Cited by 58
- Authors
- Lee, D., Takayama, S., & Goldberg, A. L.
- Affiliations
- Department of Cell Biology, Harvard Medical School, Boston, MA 02115;
- Research Division, Chugai Pharma USA, Berkley Heights, NJ 07922
- Harvard University (US)
- Corresponding author
- Goldberg, Alfred L.
- ORCID
- Goldberg, Alfred L.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2018-09-25
- Volume
- 115
- Issue
- 41
- Pages
- E9550-E9559
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC6187164
- OpenAlex
- W2893547115
- Cited by
- 58
- References
- 47
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 12 · 2023: 8 · 2022: 7 · 2021: 6 · 2020: 9 · 2019: 6
- FWCI
- 1.87
- Type
- journal article
- Language
- en
- Update notices
- correction (2019-01-14)
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- HHS | NIH | National Institute of General Medical Sciences (GM051923-18)
- Muscular Dystrophy Association (MDA419143)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Keywords
- 26S proteasome, proteasome activation, protein degradation, ubiquitinated proteins, ubiquitin binding, skeletal muscle atrophy
- MeSH terms
- Protein Domains, Animals, Cell-Free System, DNA-Binding Proteins, HeLa Cells, Humans, Mice, Transgenic, Recombinant Proteins, Enzyme Activators, Proteasome Endopeptidase Complex, Mice, Ubiquitination, HEK293 Cells, Proteolysis
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