UBE2O is a quality control factor for orphans of multiprotein complexes
Open accessAbstract
Removing orphan proteins from the system: The degradation of excess subunits of protein complexes is a major quality-control problem for the cell. How such “orphans” are recognized and tagged for degradation is poorly understood. Two papers identify a protein quality-control pathway that acts on some of the most abundant protein complexes in the human body: hemoglobin and ribosomes (see the Perspective by Hampton and Dargemont). Yanagitani et al. show that the central player in this process is an unusual enzyme (UBE2O) that recognizes substrates and tags them for destruction. Other quality-contr ol pathways tend to use separate factors for target selection (often a chaperone), ubiquitin donation (an E2), and ubiquitin conjugati on (an E3). Encoding all three activities in a single factor whose function can be reconstituted in a purified system provides a tractable route to detailed mechanistic and structural dissection. Nguyen et al. show the importance of the UBE2O pathway in the differentiation of red blood cells. Science , this issue p. 472 , p. 471 ; see also p. 450
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The reduction of Exo9 and EXOSC10 protein abundance across all subunits is caused by orphan protein decay because of the increased production of the unstable, and likely unusable, short EXOSC3 proteoform.
“We conclude that the reduction of Exo9 and EXOSC10 protein abundance across all subunits is caused by orphan protein decay because of the increased production of the unstable, and likely unusable, short EXOSC3 proteoform107–109.”
From EXOSC3 G191 Variants Trigger System-Wide Recalibration of RNA Processing Machinery (2026) · cites this paper as [107]
The paper’s Abstract (page unavailable) supports the general mechanism: unassembled subunits of multiprotein complexes can become orphan proteins targeted for degradation. It does not address EXOSC3 proteoforms, Exo9, or EXOSC10, so it cannot support the sentence’s specific explanation for their reduced abundance. (LLM, conf=0.86)
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References 41 · Cited by 132
- Authors
- Yanagitani, K., Juszkiewicz, S., & Hegde, R. S.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Corresponding author
- Yanagitani, Kota
- Hegde, Ramanujan S.
- Venue
- Science
- Published
- 2017-08-04
- Volume
- 357
- Issue
- 6350
- Pages
- 472-475
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC5549844
- OpenAlex
- W2744204310
- Cited by
- 132
- References
- 41
- Citations by year
- 2026: 15 · 2025: 13 · 2024: 16 · 2023: 16 · 2022: 16 · 2021: 13 · 2020: 16 · 2019: 10 · 2018: 11 · 2017: 6
- FWCI
- 4.81
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Uehara Memorial Foundation (award312985)
- Medical Research Council (award302817, MC_UP_A022_1007)
- Japan Society for the Promotion of Science (award312984)
- 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
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- UBE2O, E2 ubiquitin-conjugating enzyme, protein quality control, multiprotein complex assembly, orphan proteins, ubiquitination, protein degradation, proteostasis, reticulocytes, alpha-globin, beta-globin, ribosomal proteins, nuclear import, substrate recognition
- MeSH terms
- SEC Translocation Channels, Cytosol, Humans, Reticulocytes, Ribosomal Proteins, Active Transport, Cell Nucleus, Ubiquitin, Ubiquitin-Conjugating Enzymes, Multiprotein Complexes, Ubiquitination, alpha-Globins, beta-Globins, HEK293 Cells, Hydrophobic and Hydrophilic Interactions, Proteolysis
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