Evidence map›Paper›PMID 21607647›Full record

ArticleMolecules and cells2011

Identification and molecular properties of SUMO-binding proteins in Arabidopsis.

Hyeong Cheol Park, Wonkyun Choi, Hee Jin Park, Mi Sun Cheong, Yoon Duck Koo, Gilok Shin, Woo Sik Chung, Woe-Yeon Kim, Min Gab Kim, Ray A Bressan and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecules and cells, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

23 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Protein sumoylation and phosphorylation intersect in Arabidopsis signaling.The Plant journal : for cell and molecular biology · 2017
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. SUMOylation of phytochrome-B negatively regulates light-induced signaling in Arabidopsis thaliana.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  13. Review
  14. Identification of sumoylated proteins in the silkworm Bombyx mori.International journal of molecular sciences · 2014
    Article
  15. Article
  16. Identification of Arabidopsis SUMO-interacting proteins that regulate chromatin activity and developmental transitions.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  17. Review
  18. Emerging role of SUMOylation in plant development.Plant signaling & behavior · 2013
    Review
  19. Cold signaling and cold response in plants.International journal of molecular sciences · 2013
    Article
  20. In vivo localization and identification of SUMOylated proteins in the brain of His6-HA-SUMO1 knock-in mice.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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

13 authors at 4 institutions in 3 countries.

Hyeong Cheol ParkDivision of Applied Life Science (Brain Korea 21 Program), and Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, Jinju 660-701, Korea. hcpark@gnu.ac.kr
Wonkyun Choi
Hee Jin Park
Mi Sun Cheong
Yoon Duck Koo
Gilok Shin
Woo Sik Chung
Woe-Yeon Kim
Min Gab Kim
Ray A Bressan
Hans J Bohnert
Sang Yeol Lee
Dae-Jin Yun
Gyeongsang National University · KRPurdue University West Lafayette · USRural Development Administration · KRUniversity of Illinois Urbana-Champaign · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reversible conjugation of the small ubiquitin modifier (SUMO) peptide to proteins (SUMOylation) plays important roles in cellular processes in animals and yeasts. However, little is known about plant SUMO targets. To identify SUMO substrates in Arabidopsis and to probe for biological functions of SUMO proteins, we constructed 6xHis-3xFLAG fused AtSUMO1 (HFAtSUMO1) controlled by the CaMV35S promoter for transformation into Arabidopsis Col-0. After heat treatment, an increased sumoylation pattern was detected in the transgenic plants. SUMO1-modified proteins were selected after two-dimensional gel electrophoresis (2-DE) image analysis and identified using matrix-assisted laser-desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS). We identified 27 proteins involved in a variety of processes such as nucleic acid metabolism, signaling, metabolism, and including proteins of unknown functions. Binding and sumoylation patterns were confirmed independently. Surprisingly, MCM3 (At5G46280), a DNA replication licensing factor, only interacted with and became sumoylated by AtSUMO1, but not by SUMO1ΔGG or AtSUMO3. The results suggest specific interactions between sumoylation targets and particular sumoylation enzymes.

Indexed as

ArabidopsisArabidopsis ProteinsCell DifferentiationCells, CulturedHot TemperatureMutant ProteinsNucleic AcidsPlant RootsProtein BindingProtein EngineeringProtein Processing, Post-TranslationalProteomicsRecombinant Fusion ProteinsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSubstrate SpecificityArabidopsis ProteinsMutant ProteinsNucleic AcidsRecombinant Fusion ProteinsSUM1 protein, Arabidopsis

Identifiers

PMID21607647
PMCPMC3887670
OpenAlexW2034126114

What OpenQuestion holds

Textmetadata
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.