Evidence map›Paper›PMID 22509284›Full record

ArticlePloS one2012

Phosphorylation of Ubc9 by Cdk1 enhances SUMOylation activity.

Yee-Fun Su, Tsunghan Yang, Hoting Huang, Leroy F Liu, Jaulang Hwang

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

29 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. SUMO: From Bench to Bedside.Physiological reviews · 2020
    Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. SUMO and the robustness of cancer.Nature reviews. Cancer · 2017
    Review
  16. Article
  17. SUMOylation regulates the intracellular fate of ZO-2.Cellular and molecular life sciences : CMLS · 2017
    Article
  18. Inhibition of CDK1 activity by sumoylation.Biochemical and biophysical research communications · 2016
    Article
  19. Article
  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

5 authors at 2 institutions in 1 country.

Yee-Fun SuMolecular and Cell Biology Program, Graduate Institute of Life Sciences, National Defense Medical Center, Academia Sinica, Taipei, Taiwan.
Tsunghan Yang
Hoting Huang
Leroy F Liu
Jaulang Hwang
Institute of Molecular Biology, Academia Sinica · TWNational Defense Medical Center · TW

Funding

MECHANISMS OF ACTION IN ANTITUMOR DRUGSR01CA039662 · NCI · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI LIU, LEROY F · 1985 to 2013
$3.8M
NCI NIH HHS CA39662NCI NIH HHS R01 CA039662
6 · The paper itself

Abstract

Increasing evidence has pointed to an important role of SUMOylation in cell cycle regulation, especially for M phase. In the current studies, we have obtained evidence through in vitro studies that the master M phase regulator CDK1/cyclin B kinase phosphorylates the SUMOylation machinery component Ubc9, leading to its enhanced SUMOylation activity. First, we show that CDK1/cyclin B, but not many other cell cycle kinases such as CDK2/cyclin E, ERK1, ERK2, PKA and JNK2/SAPK1, specifically enhances SUMOylation activity. Second, CDK1/cyclin B phosphorylates the SUMOylation machinery component Ubc9, but not SAE1/SAE2 or SUMO1. Third, CDK1/cyclin B-phosphorylated Ubc9 exhibits increased SUMOylation activity and elevated accumulation of the Ubc9-SUMO1 thioester conjugate. Fourth, CDK1/cyclin B enhances SUMOylation activity through phosphorylation of Ubc9 at serine 71. These studies demonstrate for the first time that the cell cycle-specific kinase CDK1/cyclin B phosphorylates a SUMOylation machinery component to increase its overall SUMOylation activity, suggesting that SUMOylation is part of the cell cycle program orchestrated by CDK1 through Ubc9.

Indexed as

SumoylationAmino Acid SequenceAnimalsCDC2 Protein KinaseCell CycleCell LineCyclin BDNA Topoisomerases, Type IHumansMolecular Sequence DataPhosphorylationSerineSubstrate SpecificitySulfhydryl CompoundsUbiquitin-Activating EnzymesUbiquitin-Conjugating EnzymesCDC2 Protein KinaseCyclin BDNA Topoisomerases, Type ISerineSulfhydryl CompoundsUbiquitin-Activating EnzymesUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9

Identifiers

PMID22509284
PMCPMC3317942
OpenAlexW2035665453

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.