Evidence map›Paper›PMID 31485003›Full record

ArticleNature communications2019

The poly-SUMO2/3 protease SENP6 enables assembly of the constitutive centromere-associated network by group deSUMOylation.

Frauke Liebelt, Nicolette S Jansen, Sumit Kumar, Ekaterina Gracheva, Laura A Claessens, Matty Verlaan-de Vries, Edwin Willemstein, Alfred C O Vertegaal

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

48 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Preserving centromere identity: right amounts of CENP-A at the right place and time.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025
    Review
  9. Article
  10. Article
  11. Solo or in Concert: SUMOylation in Pathogenic Fungi.The plant pathology journal · 2025
    Review
  12. Article
  13. Article
  14. Review
  15. Multifaceted roles of SUMO in DNA metabolism.Nucleus (Austin, Tex.) · 2024
    Review
  16. Article
  17. SUMO and the DNA damage response.Biochemical Society transactions · 2024
    Review
  18. Article
  19. Article
  20. 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

8 authors at 1 institution in 1 country.

Frauke LiebeltCell and Chemical Biology, Leiden University Medical Center, Leiden, The Netherlands.
Nicolette S JansenCell and Chemical Biology, Leiden University Medical Center, Leiden, The Netherlands.
Sumit KumarCell and Chemical Biology, Leiden University Medical Center, Leiden, The Netherlands.ORCID http://orcid.org/0000-0003-0102-0567
Ekaterina GrachevaCell and Chemical Biology, Leiden University Medical Center, Leiden, The Netherlands.
Laura A ClaessensCell and Chemical Biology, Leiden University Medical Center, Leiden, The Netherlands.
Matty Verlaan-de VriesCell and Chemical Biology, Leiden University Medical Center, Leiden, The Netherlands.
Edwin WillemsteinCell and Chemical Biology, Leiden University Medical Center, Leiden, The Netherlands.
Alfred C O VertegaalCell and Chemical Biology, Leiden University Medical Center, Leiden, The Netherlands. vertegaal@lumc.nl.ORCID http://orcid.org/0000-0002-7989-0493
Leiden University Medical Center · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In contrast to our extensive knowledge on ubiquitin polymer signaling, we are severely limited in our understanding of poly-SUMO signaling. We set out to identify substrates conjugated to SUMO polymers, using knockdown of the poly-SUMO2/3 protease SENP6. We identify over 180 SENP6 regulated proteins that represent highly interconnected functional groups of proteins including the constitutive centromere-associated network (CCAN), the CENP-A loading factors Mis18BP1 and Mis18A and DNA damage response factors. Our results indicate a striking protein group de-modification by SENP6. SENP6 deficient cells are severely compromised for proliferation, accumulate in G2/M and frequently form micronuclei. Accumulation of CENP-T, CENP-W and CENP-A to centromeres is impaired in the absence of SENP6. Surprisingly, the increase of SUMO chains does not lead to ubiquitin-dependent proteasomal degradation of the CCAN subunits. Our results indicate that SUMO polymers can act in a proteolysis-independent manner and consequently, have a more diverse signaling function than previously expected.

Indexed as

Protein Interaction MapsProtein Processing, Post-TranslationalCell Line, TumorCell ProliferationCentromereCentromere Protein AChromosomal Proteins, Non-HistoneCysteine EndopeptidasesHEK293 CellsHeLa CellsHumansRNA InterferenceSmall Ubiquitin-Related Modifier ProteinsSumoylationUbiquitinsCentromere Protein AChromosomal Proteins, Non-HistoneCysteine EndopeptidasesSENP6 protein, humanSmall Ubiquitin-Related Modifier ProteinsSUMO2 protein, humanSUMO3 protein, humanUbiquitins

Identifiers

PMID31485003
PMCPMC6726658
OpenAlexW2971643529

What OpenQuestion holds

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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.