Evidence map›Paper›PMID 23874224›Full record

ArticlePLoS genetics2013

The arabidopsis RNA binding protein with K homology motifs, SHINY1, interacts with the C-terminal domain phosphatase-like 1 (CPL1) to repress stress-inducible gene expression.

Jiafu Jiang, Bangshing Wang, Yun Shen, Hui Wang, Qing Feng, Huazhong Shi

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.7field-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

37 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Article
  3. RNA-binding proteins orchestrating immunity in plants.The Plant journal : for cell and molecular biology · 2025
    Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Emerging Roles of RNA-Binding Proteins in Seed Development and Performance.International journal of molecular sciences · 2020
    Review
  17. Article
  18. 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

6 authors at 1 institution in 1 country.

Jiafu JiangDepartment of Chemistry and Biochemistry, Center for Chemical Biology, Texas Tech University, Lubbock, Texas, USA.
Bangshing Wang
Yun Shen
Hui Wang
Qing Feng
Huazhong Shi
Texas Tech University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The phosphorylation state of the C-terminal domain (CTD) of the RNA polymerase II plays crucial roles in transcription and mRNA processing. Previous studies showed that the plant CTD phosphatase-like 1 (CPL1) dephosphorylates Ser-5-specific CTD and regulates abiotic stress response in Arabidopsis. Here, we report the identification of a K-homology domain-containing protein named SHINY1 (SHI1) that interacts with CPL1 to modulate gene expression. The shi1 mutant was isolated from a forward genetic screening for mutants showing elevated expression of the luciferase reporter gene driven by a salt-inducible promoter. The shi1 mutant is more sensitive to cold treatment during vegetative growth and insensitive to abscisic acid in seed germination, resembling the phenotypes of shi4 that is allelic to the cpl1 mutant. Both SHI1 and SHI4/CPL1 are nuclear-localized proteins. SHI1 interacts with SHI4/CPL1 in vitro and in vivo. Loss-of-function mutations in shi1 and shi4 resulted in similar changes in the expression of some stress-inducible genes. Moreover, both shi1 and shi4 mutants display higher mRNA capping efficiency and altered polyadenylation site selection for some of the stress-inducible genes, when compared with wild type. We propose that the SHI1-SHI4/CPL1 complex inhibits transcription by preventing mRNA capping and transition from transcription initiation to elongation.

Indexed as

Gene Expression Regulation, PlantAbscisic AcidArabidopsisArabidopsis ProteinsMutationPhosphoprotein PhosphatasesPhosphoric Monoester HydrolasesProtein Structure, TertiaryRNA-Binding ProteinsRNA Polymerase IIRNA Processing, Post-TranscriptionalTranscription FactorsTranscription, GeneticAbscisic AcidArabidopsis ProteinsCPL1 protein, ArabidopsisPhosphoprotein PhosphatasesPhosphoric Monoester HydrolasesRCF3 protein, ArabidopsisRNA-Binding ProteinsRNA Polymerase IITranscription Factors

Identifiers

PMID23874224
PMCPMC3708844
OpenAlexW2011793652

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.