Evidence map›Paper›PMID 24468197›Full record

ArticleBMC systems biology2014

Tetramer formation in Arabidopsis MADS domain proteins: analysis of a protein-protein interaction network.

Carlos Espinosa-Soto, Richard Gh Immink, Gerco C Angenent, Elena R Alvarez-Buylla, Stefan de Folter

Open access · diamondAbstract read
In one paragraph

Article in BMC systems biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
7.5field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

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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

11 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Article
  3. Cracking the Floral Quartet Code: How Do Multimers of MIKCInternational journal of molecular sciences · 2023
    Review
  4. Article
  5. Overexpression of MADS-box GenePlants (Basel, Switzerland) · 2020
    Article
  6. Article
  7. Structural Basis for Plant MADS Transcription Factor Oligomerization.Computational and structural biotechnology journal · 2019
    Review
  8. Review
  9. Article
  10. Article
  11. 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 3 institutions in 2 countries.

Carlos Espinosa-Soto
Richard Gh Immink
Gerco C Angenent
Elena R Alvarez-BuyllaLaboratorio Nacional de Genómica para la Biodiversidad (Langebio), Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (CINVESTAV-IPN), Km 9,6 Libramiento Norte Carretera León, C,P, 36821 Irapuato, Mexico. eabuylla@gmail.com.
Stefan de Folter
Center for Research and Advanced Studies of the National Polytechnic Institute · MXUniversidad Nacional Autónoma de México · MXWageningen University & Research · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundMADS domain proteins are transcription factors that coordinate several important developmental processes in plants. These proteins interact with other MADS domain proteins to form dimers, and it has been proposed that they are able to associate as tetrameric complexes that regulate transcription of target genes. Whether the formation of functional tetramers is a widespread property of plant MADS domain proteins, or it is specific to few of these transcriptional regulators remains unclear.

resultsWe analyzed the structure of the network of physical interactions among MADS domain proteins in Arabidopsis thaliana. We determined the abundance of subgraphs that represent the connection pattern expected for a MADS domain protein heterotetramer. These subgraphs were significantly more abundant in the MADS domain protein interaction network than in randomized analogous networks. Importantly, these subgraphs are not significantly frequent in a protein interaction network of TCP plant transcription factors, when compared to expectation by chance. In addition, we found that MADS domain proteins in tetramer-like subgraphs are more likely to be expressed jointly than proteins in other subgraphs. This effect is mainly due to proteins in the monophyletic MIKC clade, as there is no association between tetramer-like subgraphs and co-expression for proteins outside this clade.

conclusionsOur results support that the tendency to form functional tetramers is widespread in the MADS domain protein-protein interaction network. Our observations also suggest that this trend is prevalent, or perhaps exclusive, for proteins in the MIKC clade. Because it is possible to retrodict several experimental results from our analyses, our work can be an important aid to make new predictions and facilitates experimental research on plant MADS domain proteins.

Indexed as

Protein Interaction MapsProtein MultimerizationArabidopsisArabidopsis ProteinsGene Expression Regulation, PlantMADS Domain ProteinsProtein Structure, QuaternaryArabidopsis ProteinsMADS Domain Proteins

Identifiers

PMID24468197
PMCPMC3913338
OpenAlexW2149900894

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.