Evidence map›Paper›PMID 40132582›Full record

ArticleMolecular cell2025

UbiREAD deciphers proteasomal degradation code of homotypic and branched K48 and K63 ubiquitin chains.

Leo Kiss, Leo C James, Brenda A Schulman

Abstract read
In one paragraph

Article in Molecular cell, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

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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

18 citing papers in PubMed.

  1. Review
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  14. Review
  15. Article
  16. Targeting ubiquitination in disease and therapy.Signal transduction and targeted therapy · 2025
    Review
  17. Review
  18. Decoding ubiquitin signals inside cells.Nature reviews. Molecular cell biology · 2025
    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

3 authors.

Leo KissDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried 82152, Germany. Electronic address: lkiss@biochem.mpg.de.
Leo C JamesMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Brenda A SchulmanDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.

Funding

Medical Research Council MC_U105181010Wellcome Trust 223054
6 · The paper itself

Abstract

Ubiquitin chains define the fates of their modified proteins, often mediating proteasomal degradation in eukaryotes. Yet heterogeneity of intracellular ubiquitination has precluded systematically comparing the degradation capacities of different ubiquitin chains. We developed ubiquitinated reporter evaluation after intracellular delivery (UbiREAD), a technology that monitors cellular degradation and deubiquitination at high temporal resolution after bespoke ubiquitinated proteins are delivered into human cells. Comparing the degradation of a model substrate modified with various K48, K63, or K48/K63-branched ubiquitin chains revealed fundamental differences in their intracellular degradation capacities. K48 chains with three or more ubiquitins triggered degradation within minutes. K63-ubiquitinated substrate was rapidly deubiquitinated rather than degraded. Surprisingly, in K48/K63-branched chains, substrate-anchored chain identity determined the degradation and deubiquitination behavior, establishing that branched chains are not the sum of their parts. UbiREAD reveals a degradation code for ubiquitin chains varying by linkage, length, and topology and a functional hierarchy within branched ubiquitin chains.

Indexed as

LysineProteasome Endopeptidase ComplexUbiquitinHEK293 CellsHeLa CellsHumansProteolysisUbiquitinationLysineProteasome Endopeptidase ComplexUbiquitinbranched ubiquitin chainsdeubiquitinationelectroporationK48K63proteasomeprotein degradationproteostasisubiquitinubiquitin code

Identifiers

PMID40132582
PMCPMC7617769

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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.