Building ubiquitin chains: E2 enzymes at work
Open accessAbstract
The modification of proteins with ubiquitin chains can change their localization, activity and/or stability. Although ubiquitylation requires the concerted action of ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s), it is the E2s that have recently emerged as key mediators of chain assembly. These enzymes are able to govern the switch from ubiquitin chain initiation to elongation, regulate the processivity of chain formation and establish the topology of assembled chains, thereby determining the consequences of ubiquitylation for the modified proteins.
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Most E2 ligases have a preference for forming specific polyubiquitin chain linkages.
“as most E2 ligases have a preference for forming specific polyubiquitin chain linkages (24,25).”
From Distinct Functional Domains Contribute to Degradation of the Low Density Lipoprotein Receptor (LDLR) by the E3 Ubiquitin Ligase Inducible Degrader of the LDLR (IDOL) (2011) · cites this paper as [24]
In “Selecting the correct linkage” (page not supplied), the review says that many E2s have intrinsic linkage specificity and gives examples with distinct preferred linkages. It does not establish that most E2s do, and it identifies the UBE2D family as an exception. The source calls E2s ubiquitin-conjugating enzymes, not ligases. (LLM, conf=0.85)
Experimental — accuracy not yet measuredDifferential E2 ligase recruitment to IDOL determines the outcome of the ubiquitination reaction.
“However, we find it more plausible that differential E2 ligase recruitment to IDOL determines the outcome of the ubiquitination reaction as most E2 ligases have a preference for forming specific polyubiquitin chain linkages (24,25).”
The E2 enzyme, rather than the E3 scaffold, dictates the type and length of ubiquitin linkage formed.
“This is important, because it is the E2 enzyme (rather than the E3 scaffold itself) that dictates the type and length of ubiquitin linkage formed [22].”
From The p53 orchestra: Mdm2 and Mdmx set the tone (2010) · cites this paper as [22]
The inability to identify the intracellular E2s needed for p53 ubiquitylation in vivo is likely explained by weak and short-lived E2-E3 contacts.
“This is probably due to the low affinity and the transient nature of E2–E3 interactions120,121.”
From MDM2, MDMX and p53 in oncogenesis and cancer therapy (2013) · cites this paper as [120]
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- Authors
- Ye, Y., & Rape, M.
- Affiliations
- National Institutes of Health (US)
- ORCID
- Ye, Yihong
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2009-11
- Volume
- 10
- Issue
- 11
- Pages
- 755-764
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- PMC
- PMC3107738
- OpenAlex
- W2028157992
- Cited by
- 989
- References
- 95
- Citations by year
- 2026: 35 · 2025: 44 · 2024: 69 · 2023: 48 · 2022: 55 · 2021: 73 · 2020: 53 · 2019: 62 · 2018: 39 · 2017: 57 · 2016: 57 · 2015: 60 · 2014: 71 · 2013: 76 · 2012: 75
- FWCI
- 4.79
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM083064)
- National Institute of Diabetes and Digestive and Kidney Diseases (ZIADK036137)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Keywords
- E2 ubiquitin-conjugating enzyme, ubiquitin chain assembly, ubiquitin chain elongation, processivity, chain topology, ubiquitination, E1 enzyme, E3 ubiquitin ligase, protein modification
- MeSH terms
- Animals, Humans, Ubiquitin, Ubiquitin-Conjugating Enzymes
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