Evidence map›Paper›PMID 40463067›Full record

ArticlebioRxiv : the preprint server for biology2025

A complete map of human cytosolic degrons and their relevance for disease.

Vasileios Voutsinos, Kristoffer E Johansson, Fia B Larsen, Martin Grønbæk-Thygesen, Nicolas Jonsson, Emma Holm-Olesen, Giulio Tesei, Amelie Stein, Douglas M Fowler, Kresten Lindorff-Larsen and 1 more

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors.

Vasileios VoutsinosLinderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK2200N Copenhagen, Denmark.ORCID 0000-0002-0911-3648
Kristoffer E JohanssonLinderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK2200N Copenhagen, Denmark.ORCID 0000-0001-6054-0461
Fia B LarsenLinderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK2200N Copenhagen, Denmark.
Martin Grønbæk-ThygesenLinderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK2200N Copenhagen, Denmark.ORCID 0000-0001-6132-8243
Nicolas JonssonLinderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK2200N Copenhagen, Denmark.ORCID 0000-0002-7838-1814
Emma Holm-OlesenLinderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK2200N Copenhagen, Denmark.
Giulio TeseiLinderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK2200N Copenhagen, Denmark.ORCID 0000-0003-4339-4460
Amelie SteinDepartment of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK2200N Copenhagen, Copenhagen, Denmark.ORCID 0000-0002-5862-1681
Douglas M FowlerDepartment of Genome Sciences, University of Washington, Seattle, WA, USA.ORCID 0000-0001-7614-1713
Kresten Lindorff-LarsenLinderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK2200N Copenhagen, Denmark.ORCID 0000-0002-4750-6039
Rasmus Hartmann-PetersenLinderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK2200N Copenhagen, Denmark.ORCID 0000-0002-4155-7791

Funding

New approaches for investigating the causes and consequences of cellular heterogeneityR35GM152106 · NIGMS · UNIVERSITY OF WASHINGTON · PI Douglas M Fowler · 2024 to 2026
$1.8M
NIGMS NIH HHS R35 GM152106
6 · The paper itself

Abstract

Degrons are short protein segments that target proteins for degradation via the ubiquitin-proteasome system and thus ensure timely removal of signaling proteins and clearance of misfolded proteins from the intracellular space. Here, we describe a systematic screen for degrons in the human cytosol. We determine degron potency of >200,000 different 30-residue tiles from more than 5,000 cytosolic human proteins with 99.7% coverage. In total, 19.1% of the tiles function as strong degrons, 30.4% as intermediate degrons, while 50.5% did not display degron properties. The vast majority of the degrons are dependent on the E1 ubiquitin-activating enzyme and the proteasome but independent of autophagy. The results reveal both known and novel degron motifs, both internal as well as at the C-terminus. Mapping the degrons onto protein structures, predicted by AlphaFold2, revealed that most of the degrons are located in buried regions, indicating that they only become active upon unfolding or misfolding. Training of a machine learning model allowed us to probe the degron properties further and predict the cellular abundance of missense variants that operate by forming degrons in exposed and disordered protein regions, thus providing a mechanism of pathogenicity for germline coding variants at such positions.

Indexed as

chaperonedeep mutational scanningDMSE3gene variantsproteasomeprotein degradationprotein foldingprotein quality controlprotein stabilityubiquitin

Identifiers

PMID40463067
PMCPMC12132302

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.