Evidence map›Paper›PMID 35027744›Full record

ArticleNature chemical biology2022

Structure of UBE2K-Ub/E3/polyUb reveals mechanisms of K48-linked Ub chain extension.

Mark A Nakasone, Karolina A Majorek, Mads Gabrielsen, Gary J Sibbet, Brian O Smith, Danny T Huang

Open access · hybridAbstract read
In one paragraph

Article in Nature chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.9field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

31 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
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  4. [Ubiquitination-mediated regulation of T cell homeostasis and autoimmune diseases].Zhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences · 2026
    Review
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  19. Chemical Tools for Probing the Ub/Ubl Conjugation Cascades.Chembiochem : a European journal of chemical biology · 2025
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Mark A Nakasone *Cancer Research UK Beatson Institute, Glasgow, UK.ORCID http://orcid.org/0000-0002-1362-191X
Karolina A Majorek *Cancer Research UK Beatson Institute, Glasgow, UK.
Mads GabrielsenCancer Research UK Beatson Institute, Glasgow, UK.ORCID http://orcid.org/0000-0002-9848-2276
Gary J SibbetCancer Research UK Beatson Institute, Glasgow, UK.
Brian O SmithInstitute of Molecular Cell and System Biology, University of Glasgow, Glasgow, UK.ORCID http://orcid.org/0000-0003-3363-4168
Danny T HuangCancer Research UK Beatson Institute, Glasgow, UK. d.huang@beatson.gla.ac.uk.ORCID http://orcid.org/0000-0002-6192-259X
Cancer Research UK Scotland Institute · GBUniversity of Glasgow · GB

Funding

Cancer Research UK 23278Cancer Research UK 29256Cancer Research UK A23278Cancer Research UK A31287Cancer Research UK C596/A17196European Research Council 647849
6 · The paper itself

Abstract

Ubiquitin (Ub) chain types govern distinct biological processes. K48-linked polyUb chains target substrates for proteasomal degradation, but the mechanism of Ub chain synthesis remains elusive due to the transient nature of Ub handover. Here, we present the structure of a chemically trapped complex of the E2 UBE2K covalently linked to donor Ub and acceptor K48-linked di-Ub, primed for K48-linked Ub chain synthesis by a RING E3. The structure reveals the basis for acceptor Ub recognition by UBE2K active site residues and the C-terminal Ub-associated (UBA) domain, to impart K48-linked Ub specificity and catalysis. Furthermore, the structure unveils multiple Ub-binding surfaces on the UBA domain that allow distinct binding modes for K48- and K63-linked Ub chains. This multivalent Ub-binding feature serves to recruit UBE2K to ubiquitinated substrates to overcome weak acceptor Ub affinity and thereby promote chain elongation. These findings elucidate the mechanism of processive K48-linked polyUb chain formation by UBE2K.

Indexed as

PolyubiquitinUbiquitinProtein BindingProtein DomainsUbiquitinationUbiquitin-Conjugating EnzymesPolyubiquitinUbiquitinUbiquitin-Conjugating Enzymes

Identifiers

PMID35027744
PMCPMC8964413
OpenAlexW4206527354

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.