Evidence map›Paper›PMID 42206743›Full record

ReviewFEBS letters2026

The ubiquitin-proteasome system and autophagy as guardians of the cellular proteome.

Ivan Dikic

Abstract readReview
In one paragraph

Review in FEBS letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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

1 author.

Ivan DikicInstitute of Biochemistry II, Goethe University Medical Faculty, Frankfurt am Main, Germany.ORCID https://orcid.org/0000-0001-8156-9511

Funding

Deutsche Forschungsgemeinschaft 259130777 - SFB 1177Deutsche Forschungsgemeinschaft TRR 387/1 - 514894665H2020 European Research Council ER-REMODEL 101055213
6 · The paper itself

Abstract

Maintaining a functional proteome is essential for cellular health and organismal longevity. Disruption of proteostasis is a hallmark of aging and a central driver of diverse pathologies, including neurodegeneration, cancer, and metabolic disease. The ubiquitin-proteasome system (UPS) and autophagy represent the two principal degradative pathways safeguarding proteome integrity, particularly under conditions of stress. While historically viewed as mechanistically distinct, it is now clear that UPS and autophagy operate as an interconnected and adaptive network. This Perspective discusses three core principles that govern their coordination: (1) a shared molecular language of ubiquitin signals and shuttle proteins that determines cargo routing; (2) spatial compartmentalization through organelle-specific quality control modules and phase-separated degradation hubs; and (3) temporal regulation by stress-responsive signaling pathways that reprogram proteolytic output. Understanding this dynamic partnership not only reveals fundamental organizing principles of cellular homeostasis but also identifies new therapeutic nodes for diseases driven by proteostasis collapse.

Indexed as

AutophagyProteasome Endopeptidase ComplexProteomeUbiquitinAnimalsHumansProteolysisProteostasisProteotoxic StressSignal TransductionProteasome Endopeptidase ComplexProteomeUbiquitinautophagyER quality controlphase separationproteasomeproteostasisubiquitin

Identifiers

PMID42206743
PMCPMC13358443

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.