Evidence map›Paper›PMID 38803224›Full record

ArticleLife science alliance2024

K48- and K63-linked ubiquitin chain interactome reveals branch- and length-specific ubiquitin interactors.

Anita Waltho, Oliver Popp, Christopher Lenz, Lukas Pluska, Mahil Lambert, Volker Dötsch, Philipp Mertins, Thomas Sommer

Abstract read
In one paragraph

Article in Life science alliance, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
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

27 citing papers in PubMed.

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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

8 authors.

Anita WalthoMax Delbrück Center for Molecular Medicine in the Helmholtz Association, Berlin, Germany aswaltho@hotmail.com.ORCID 0009-0000-0059-9357
Oliver PoppMax Delbrück Center for Molecular Medicine in the Helmholtz Association, Berlin, Germany.
Christopher LenzInstitute for Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Frankfurt, Germany.ORCID 0009-0000-2261-2823
Lukas PluskaMax Delbrück Center for Molecular Medicine in the Helmholtz Association, Berlin, Germany.
Mahil LambertInstitute for Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Frankfurt, Germany.
Volker DötschInstitute for Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Frankfurt, Germany.ORCID 0000-0001-5720-212X
Philipp MertinsMax Delbrück Center for Molecular Medicine in the Helmholtz Association, Berlin, Germany.ORCID 0000-0002-2245-528X
Thomas SommerMax Delbrück Center for Molecular Medicine in the Helmholtz Association, Berlin, Germany tsommer@mdc-berlin.de.ORCID 0000-0001-9990-5202

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ubiquitin (Ub) code denotes the complex Ub architectures, including Ub chains of different lengths, linkage types, and linkage combinations, which enable ubiquitination to control a wide range of protein fates. Although many linkage-specific interactors have been described, how interactors are able to decode more complex architectures is not fully understood. We conducted a Ub interactor screen, in humans and yeast, using Ub chains of varying lengths, as well as homotypic and heterotypic branched chains of the two most abundant linkage types-lysine 48-linked (K48) and lysine 63-linked (K63) Ub. We identified some of the first K48/K63-linked branch-specific Ub interactors, including histone ADP-ribosyltransferase PARP10/ARTD10, E3 ligase UBR4, and huntingtin-interacting protein HIP1. Furthermore, we revealed the importance of chain length by identifying interactors with a preference for Ub3 over Ub2 chains, including Ub-directed endoprotease DDI2, autophagy receptor CCDC50, and p97 adaptor FAF1. Crucially, we compared datasets collected using two common deubiquitinase inhibitors-chloroacetamide and N-ethylmaleimide. This revealed inhibitor-dependent interactors, highlighting the importance of inhibitor consideration during pulldown studies. This dataset is a key resource for understanding how the Ub code is read.

Indexed as

LysineUbiquitinUbiquitinationHumansProtein BindingSaccharomyces cerevisiaeUbiquitin-Protein LigasesLysineUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID38803224
PMCPMC11109483

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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.