Evidence map›Paper›PMID 34239127›Full record

ArticleNature chemical biology2021

K29-linked ubiquitin signaling regulates proteotoxic stress response and cell cycle.

Yuanyuan Yu, Qingyun Zheng, Satchal K Erramilli, Man Pan, Seongjin Park, Yuan Xie, Jingxian Li, Jingyi Fei, Anthony A Kossiakoff, Lei Liu and 1 more

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed, 1 pooled it
4.6field-weighted citation impact, top 4% 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

49 citing papers in PubMed, 1 synthesis or guideline pooled it, 81 citations in OpenAlex.

  1. Pooled it
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  5. ALKBH5/IGF2BP1-mediated mCell biology and toxicology · 2026
    Article
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  17. The Molecular Toolbox for Linkage Type-Specific Analysis of Ubiquitin Signaling.Chembiochem : a European journal of chemical biology · 2025
    Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 4 institutions in 2 countries.

Yuanyuan Yu *Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL, USA.
Qingyun Zheng *Tsinghua-Peking Center for Life Sciences, Department of Chemistry, Tsinghua University, Beijing, China.
Satchal K Erramilli *Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL, USA.ORCID http://orcid.org/0000-0001-8694-7681
Man Pan *Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL, USA. panm@uchicago.edu.ORCID http://orcid.org/0000-0001-7216-8193
Seongjin ParkDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL, USA.
Yuan XieDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL, USA.ORCID http://orcid.org/0000-0001-5105-7136
Jingxian LiDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL, USA.
Jingyi FeiDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL, USA.ORCID http://orcid.org/0000-0002-9775-3820
Anthony A KossiakoffDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL, USA. koss@bsd.uchicago.edu.
Lei LiuTsinghua-Peking Center for Life Sciences, Department of Chemistry, Tsinghua University, Beijing, China. lliu@mail.tsinghua.edu.cn.ORCID http://orcid.org/0000-0001-6290-8602
Minglei ZhaoDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL, USA. mlzhao@uchicago.edu.ORCID http://orcid.org/0000-0001-5832-6060
University of Chicago · USUniversity of Illinois Chicago · USCenter for Life Sciences · CNKing Center · US

Funding

Chaperone-Assisted Structure Determination of Membrane ProteinsR01GM117372 · NIGMS · UNIVERSITY OF CHICAGO · PI ANTHONY A KOSSIAKOFF · 2016 to 2026
$4.0M
NIGMS NIH HHS R01 GM117372
6 · The paper itself

Abstract

Protein ubiquitination shows remarkable topological and functional diversity through the polymerization of ubiquitin via different linkages. Deciphering the cellular ubiquitin code is of central importance to understand the physiology of the cell. However, our understanding of its function is rather limited due to the lack of specific binders as tools to detect K29-linked polyubiquitin. In this study, we screened and characterized a synthetic antigen-binding fragment, termed sAB-K29, that can specifically recognize K29-linked polyubiquitin using chemically synthesized K29-linked diubiquitin. We further determined the crystal structure of this fragment bound to the K29-linked diubiquitin, which revealed the molecular basis of specificity. Using sAB-K29 as a tool, we uncovered that K29-linked ubiquitination is involved in different kinds of cellular proteotoxic stress response as well as cell cycle regulation. In particular, we showed that K29-linked ubiquitination is enriched in the midbody and downregulation of the K29-linked ubiquitination signal arrests cells in G1/S phase.

Indexed as

Cell CycleCell Line, TumorHumansModels, MolecularSignal TransductionStress, PhysiologicalUbiquitinationUbiquitin-Protein LigasesUbiquitin-Protein Ligases

Identifiers

PMID34239127
PMCPMC8717942
OpenAlexW3180116683

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Registered trials

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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.