Evidence map›Paper›PMID 31519521›Full record

ArticleMolecular cell2019

SUMO-Chain-Regulated Proteasomal Degradation Timing Exemplified in DNA Replication Initiation.

Ivan Psakhye, Federica Castellucci, Dana Branzei

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.9field-weighted citation impact, top 8% of its field
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

35 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Multifaceted roles of SUMO in DNA metabolism.Nucleus (Austin, Tex.) · 2024
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Quality control of cytoplasmic proteins inside the nucleus.Computational and structural biotechnology journal · 2022
    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

3 authors at 2 institutions in 1 country.

Ivan PsakhyeIFOM, FIRC Institute of Molecular Oncology, Via Adamello 16, 20139 Milan, Italy.
Federica CastellucciIFOM, FIRC Institute of Molecular Oncology, Via Adamello 16, 20139 Milan, Italy.
Dana BranzeiIFOM, FIRC Institute of Molecular Oncology, Via Adamello 16, 20139 Milan, Italy; Istituto di Genetica Molecolare, Consiglio Nazionale delle Ricerche (IGM-CNR), Via Abbiategrasso 207, 27100 Pavia, Italy. Electronic address: dana.branzei@ifom.eu.
FIRC Institute of Molecular Oncology · ITIstituto di Genetica Molecolare · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Similar to ubiquitin, SUMO forms chains, but the identity of SUMO-chain-modified factors and the purpose of this modification remain largely unknown. Here, we identify the budding yeast SUMO protease Ulp2, able to disassemble SUMO chains, as a DDK interactor enriched at replication origins that promotes DNA replication initiation. Replication-engaged DDK is SUMOylated on chromatin, becoming a degradation-prone substrate when Ulp2 no longer protects it against SUMO chain assembly. Specifically, SUMO chains channel DDK for SUMO-targeted ubiquitin ligase Slx5/Slx8-mediated and Cdc48 segregase-assisted proteasomal degradation. Importantly, the SUMOylation-defective ddk-KR mutant rescues inefficient replication onset and MCM activation in cells lacking Ulp2, suggesting that SUMO chains time DDK degradation. Using two unbiased proteomic approaches, we further identify subunits of the MCM helicase and other factors as SUMO-chain-modified degradation-prone substrates of Ulp2 and Slx5/Slx8. We thus propose SUMO-chain/Ulp2-protease-regulated proteasomal degradation as a mechanism that times the availability of functionally engaged SUMO-modified protein pools during replication and beyond.

Indexed as

DNA ReplicationReplication OriginSumoylationCell Cycle ProteinsDNA, FungalEndopeptidasesGene Expression Regulation, FungalMutationProteasome Endopeptidase ComplexProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTime FactorsUbiquitin-Protein LigasesValosin Containing ProteinCDC48 protein, S cerevisiaeCDC7 protein, S cerevisiaeCell Cycle ProteinsDNA, FungalEndopeptidasesProteasome Endopeptidase ComplexProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSlx5 protein, S cerevisiaeSlx8 protein, S cerevisiaeUbiquitin-Protein LigasesULP2 protein, S cerevisiaeValosin Containing ProteinCdc48 segregaseDDKDNA replicationprotein-group modificationSENP/Ulp proteasesSlx5/8STUbL-mediated proteasomal degradationSUMOSUMO chainsubiquitin

Identifiers

PMID31519521
PMCPMC6891891
OpenAlexW2973226590

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.