Evidence map›Paper›PMID 27335169›Full record

ReviewAmerican journal of physiology. Cell physiology2016

Ubiquitin-dependent and independent roles of SUMO in proteostasis.

Frauke Liebelt, Alfred C O Vertegaal

Abstract readReview
In one paragraph

Review in American journal of physiology. Cell physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing 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

55 citing papers in PubMed.

  1. A Neurotensin Brake on Exploratory Drive under Persistent Threat.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. PAR-Driven Condensation Maintains Stalled Replication Fork Stability.bioRxiv : the preprint server for biology · 2026
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  16. Signalling mechanisms and cellular functions of SUMO.Nature reviews. Molecular cell biology · 2022
    Review
  17. SUMO-modifying Huntington's disease.IBRO neuroscience reports · 2022
    Review
  18. Review
  19. Review
  20. 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

2 authors.

Frauke LiebeltDepartment of Molecular Cell Biology, Leiden University Medical Center, Leiden, the Netherlands.
Alfred C O VertegaalDepartment of Molecular Cell Biology, Leiden University Medical Center, Leiden, the Netherlands vertegaal@lumc.nl.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellular proteomes are continuously undergoing alterations as a result of new production of proteins, protein folding, and degradation of proteins. The proper equilibrium of these processes is known as proteostasis, implying that proteomes are in homeostasis. Stress conditions can affect proteostasis due to the accumulation of misfolded proteins as a result of overloading the degradation machinery. Proteostasis is affected in neurodegenerative diseases like Alzheimer's disease, Parkinson's disease, and multiple polyglutamine disorders including Huntington's disease. Owing to a lack of proteostasis, neuronal cells build up toxic protein aggregates in these diseases. Here, we review the role of the ubiquitin-like posttranslational modification SUMO in proteostasis. SUMO alone contributes to protein homeostasis by influencing protein signaling or solubility. However, the main contribution of SUMO to proteostasis is the ability to cooperate with, complement, and balance the ubiquitin-proteasome system at multiple levels. We discuss the identification of enzymes involved in the interplay between SUMO and ubiquitin, exploring the complexity of this crosstalk which regulates proteostasis. These enzymes include SUMO-targeted ubiquitin ligases and ubiquitin proteases counteracting these ligases. Additionally, we review the role of SUMO in brain-related diseases, where SUMO is primarily investigated because of its role during formation of aggregates, either independently or in cooperation with ubiquitin. Detailed understanding of the role of SUMO in these diseases could lead to novel treatment options.

Indexed as

AnimalsHomeostasisHumansNeurodegenerative DiseasesProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalSUMO-1 ProteinUbiquitinUbiquitin-Protein LigasesProteasome Endopeptidase ComplexSUMO-1 ProteinUbiquitinUbiquitin-Protein Ligasesneurodegenerative diseasesprotein aggregationsproteostasisSUMOSUMO-targeted ubiquitin ligaseubiquitin

Identifiers

PMID27335169
PMCPMC5129774

What OpenQuestion holds

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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.