Evidence map›Paper›PMID 38103558›Full record

ArticleMolecular cell2024

Ubiquiton-An inducible, linkage-specific polyubiquitylation tool.

Christian Renz, Evrydiki Asimaki, Cindy Meister, Véronique Albanèse, Kirill Petriukov, Nils C Krapoth, Sabrina Wegmann, Hans-Peter Wollscheid, Ronald P Wong, Amitkumar Fulzele and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

12 citing papers in PubMed, 15 citations in OpenAlex.

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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

13 authors at 2 institutions in 2 countries.

Christian RenzInstitute of Molecular Biology (IMB) gGmbH, Ackermannweg 4, 55128 Mainz, Germany.
Evrydiki AsimakiInstitute of Molecular Biology (IMB) gGmbH, Ackermannweg 4, 55128 Mainz, Germany.
Cindy MeisterInstitute of Molecular Biology (IMB) gGmbH, Ackermannweg 4, 55128 Mainz, Germany.
Véronique AlbanèseUniversité de Paris, CNRS, Institut Jacques Monod, 75013 Paris, France.
Kirill PetriukovInstitute of Molecular Biology (IMB) gGmbH, Ackermannweg 4, 55128 Mainz, Germany.
Nils C KrapothInstitute of Molecular Biology (IMB) gGmbH, Ackermannweg 4, 55128 Mainz, Germany.
Sabrina WegmannInstitute of Molecular Biology (IMB) gGmbH, Ackermannweg 4, 55128 Mainz, Germany.
Hans-Peter WollscheidInstitute of Molecular Biology (IMB) gGmbH, Ackermannweg 4, 55128 Mainz, Germany.
Ronald P WongInstitute of Molecular Biology (IMB) gGmbH, Ackermannweg 4, 55128 Mainz, Germany.
Amitkumar FulzeleInstitute of Molecular Biology (IMB) gGmbH, Ackermannweg 4, 55128 Mainz, Germany.
Jia-Xuan ChenInstitute of Molecular Biology (IMB) gGmbH, Ackermannweg 4, 55128 Mainz, Germany.
Sébastien LéonUniversité de Paris, CNRS, Institut Jacques Monod, 75013 Paris, France.
Helle D UlrichInstitute of Molecular Biology (IMB) gGmbH, Ackermannweg 4, 55128 Mainz, Germany. Electronic address: h.ulrich@imb-mainz.de.
Institute of Molecular Biology · DECentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The posttranslational modifier ubiquitin regulates most cellular processes. Its ability to form polymeric chains of distinct linkages is key to its diverse functionality. Yet, we still lack the experimental tools to induce linkage-specific polyubiquitylation of a protein of interest in cells. Here, we introduce a set of engineered ubiquitin protein ligases and matching ubiquitin acceptor tags for the rapid, inducible linear (M1-), K48-, or K63-linked polyubiquitylation of proteins in yeast and mammalian cells. By applying the so-called "Ubiquiton" system to proteasomal targeting and the endocytic pathway, we validate this tool for soluble cytoplasmic and nuclear as well as chromatin-associated and integral membrane proteins and demonstrate how it can be used to control the localization and stability of its targets. We expect that the Ubiquiton system will serve as a versatile, broadly applicable research tool to explore the signaling functions of polyubiquitin chains in many biological contexts.

Indexed as

UbiquitinUbiquitin-Protein LigasesAnimalsMammalsPolyubiquitinProteasome Endopeptidase ComplexSignal TransductionUbiquitinationPolyubiquitinProteasome Endopeptidase ComplexUbiquitinUbiquitin-Protein LigasesdegronE3 ligaseEGFRendocytosismonoubiquitylationpolyubiquitin chain linkageproteostasissynthetic biologytargeted protein degradationubiquitin

Identifiers

PMID38103558
PMCPMC10804999
OpenAlexW4389795861

What OpenQuestion holds

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LicenceCC BY-NC
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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.