Evidence map›Paper›PMID 15592873›Full record

ArticlePlanta2005

The Arabidopsis SERK1 protein interacts with the AAA-ATPase AtCDC48, the 14-3-3 protein GF14lambda and the PP2C phosphatase KAPP.

Ingrid M Rienties, Josefien Vink, Jan Willem Borst, Eugenia Russinova, Sacco C de Vries

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Planta, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

30 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Molecular convergence by differential domain acquisition is a hallmark of chromosomal passenger complex evolution.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Function and Regulation of Chloroplast Peroxiredoxin IIE.Antioxidants (Basel, Switzerland) · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. The SERK1 receptor-like kinase regulates organ separation in Arabidopsis flowers.The Plant journal : for cell and molecular biology · 2010
    Article
  17. Article
  18. Article
  19. Article
  20. Plasma membrane receptor complexes.Plant physiology · 2008
    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

5 authors at 1 institution in 1 country.

Ingrid M RientiesLaboratory of Biochemistry, Department of Agrotechnology and Food Sciences, Wageningen University and Research Centre, Dreijenlaan 3, 6703, HA, Wageningen, The Netherlands.
Josefien Vink
Jan Willem Borst
Eugenia Russinova
Sacco C de Vries
Wageningen University & Research · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Leucine-rich repeat (LRR)-containing transmembrane receptor-like kinases (RLKs) are important components of plant signal transduction. The Arabidopsis thaliana somatic embryogenesis receptor-like kinase 1 (AtSERK1) is an LRR-RLK proposed to participate in a signal transduction cascade involved in embryo development. By yeast two-hybrid screening we identified AtCDC48, a homologue of the mammalian AAA-ATPase p97 and GF14lambda, a member of the Arabidopsis family of 14-3-3 proteins as AtSERK1 interactors. In vitro, the AtSERK1 kinase domain is able to transphosphorylate and bind both AtCDC48 and GF14lambda. In yeast, AtCDC48 interacts with GF14lambda and with the PP2C phosphatase KAPP. In plant protoplasts AtSERK1 interacts with GF14lambda.

Indexed as

14-3-3 ProteinsAdenosine TriphosphatasesArabidopsisArabidopsis ProteinsBinding SitesCell Cycle ProteinsGene Expression ProfilingPhosphoprotein PhosphatasesPhosphorylationProtein BindingProtein KinasesProtein Phosphatase 2CProtoplastsRecombinant Fusion ProteinsSignal TransductionTrans-Activators14-3-3 ProteinsAdenosine TriphosphatasesAFT1 protein, ArabidopsisArabidopsis ProteinsCell Cycle ProteinsKAPP protein, ArabidopsisPhosphoprotein PhosphatasesProtein KinasesProtein Phosphatase 2CRecombinant Fusion ProteinsSERK1 protein, ArabidopsisTrans-ActivatorsValosin Containing Protein

Identifiers

PMID15592873
OpenAlexW2160560578

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.