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Cited by 1,056

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

A Novel Ubiquitination Factor, E4, Is Involved in Multiubiquitin Chain Assembly

Open access
Koegl, Manfred, Hoppe, Thorsten, Schlenker, Stephan, Ulrich, Helle D, Mayer, Thomas U, Jentsch, Stefan·1999·Cell

Abstract

Proteins modified by multiubiquitin chains are the preferred substrates of the proteasome. Ubiquitination involves a ubiquitin-activating enzyme, E1, a ubiquitin-conjugating enzyme, E2, and often a substrate-specific ubiquitin-protein ligase, E3. Here we show that efficient multiubiquitination needed for proteasomal targeting of a model substrate requires an additional conjugation factor, named E4. This protein, previously known as UFD2 in yeast, binds to the ubiquitin moieties of preformed conjugates and catalyzes ubiquitin chain assembly in conjunction with E1, E2, and E3. Intriguingly, E4 defines a novel protein family that includes two human members and the regulatory protein NOSA from Dictyostelium required for fruiting body development. In yeast, E4 activity is linked to cell survival under stress conditions, indicating that eukaryotes utilize E4-dependent proteolysis pathways for multiple cellular functions.

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Metadata

Authors
Koegl, M., Hoppe, T., Schlenker, S., Ulrich, H. D., Mayer, T. U., & Jentsch, S.
Venue
Cell
Publisher
Elsevier BV
Published
1999-03
Volume
96
Issue
5
Pages
635-644
ISSN
0092-8674 (ISSN-L)
OpenAlex
W2131575598
Cited by
1,056
References
2
FWCI
18.49
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: A Novel Ubiquitination Factor, E4, Is Involved in Multiubiquitin Chain Assembly. https://app.cochat.ai/papers/10.1016/s0092-8674(00)80574-7
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Koegl, M., Hoppe, T., Schlenker, S., Ulrich, H. D., Mayer, T. U., & Jentsch, S. (1999). A Novel Ubiquitination Factor, E4, Is Involved in Multiubiquitin Chain Assembly. Cell. https://doi.org/10.1016/s0092-8674(00)80574-7

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.