Evidence map›Paper›PMID 27986866›Full record

ArticlePlant physiology2017

EXTRA-LARGE G PROTEINs Interact with E3 Ligases PUB4 and PUB2 and Function in Cytokinin and Developmental Processes.

Yiping Wang, Yingying Wu, Boying Yu, Zhao Yin, Yiji Xia

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
14.4field-weighted citation impact, top 2% 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

38 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. An atypical heterotrimeric Gα and its interactome suggest an extra-large role in overcoming abiotic and biotic stress.Physiology and molecular biology of plants : an international journal of functional plant biology · 2023
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. The Role of E3 Ubiquitin Ligases in Chloroplast Function.International journal of molecular sciences · 2022
    Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. How Many Faces Does the Plant U-Box E3 Ligase Have?International journal of molecular sciences · 2022
    Review
  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 1 institution in 1 country.

Yiping WangDepartment of Biology, Hong Kong Baptist University, Hong Kong, China (Y. Wang, Y. Wu, B.Y., Z.Y., Y.X.); and.
Yingying WuDepartment of Biology, Hong Kong Baptist University, Hong Kong, China (Y. Wang, Y. Wu, B.Y., Z.Y., Y.X.); and.
Boying YuDepartment of Biology, Hong Kong Baptist University, Hong Kong, China (Y. Wang, Y. Wu, B.Y., Z.Y., Y.X.); and.
Zhao YinDepartment of Biology, Hong Kong Baptist University, Hong Kong, China (Y. Wang, Y. Wu, B.Y., Z.Y., Y.X.); and.
Yiji XiaDepartment of Biology, Hong Kong Baptist University, Hong Kong, China (Y. Wang, Y. Wu, B.Y., Z.Y., Y.X.); and yxia@hkbu.edu.hk.ORCID 0000-0002-9543-8341
Hong Kong Baptist University · HK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heterotrimeric GTP-binding proteins (G proteins) composed of Gα, Gβ, and Gγ subunits are conserved signal transduction molecules in animals and plants. In Arabidopsis (Arabidopsis thaliana), there are three Gα-like proteins named EXTRA-LARGE G PROTEINs (XLGs) in addition to the canonical Gα protein GPA1. XLGs have been reported to be implicated in multiple pathways, although the underlying mechanisms of their action remain elusive. Here, we report that all three XLGs interact with two closely related plant U-box (PUB) E3 ligases, PUB2 and PUB4. Three XLGs are predominantly localized at the plasma membrane, whereas XLG2 and XLG3 also show nuclear localization. The interactions between PUB2/4 and XLGs suggest that they might function in the same pathways. Indeed, we found that a newly obtained xlg1/2/3 triple knockout mutant, the pub4 mutant, and the pub2/4 double mutant all exhibited defects in cytokinin responses, stamen development, tapetum development, and male fertility. However, the xlg single mutants and the pub2 mutant did not exhibit an obvious defect in these processes, which suggests functional redundancy among the three XLGs and between PUB2 and PUB4. Overexpressing ARR10 to enhance the cytokinin response in pub4 or in the xlg1/2/3 triple mutant partially restored several phenotypes caused by the pub4 and xlg1/2/3 mutations. Our findings reveal that the XLGs and PUB2/4 are components in the complex cytokinin signaling networks regulating many developmental and physiological processes.

Indexed as

ArabidopsisArabidopsis ProteinsCytokininsDNA-Binding ProteinsFlowersGTP-Binding ProteinsHeterotrimeric GTP-Binding ProteinsMutationPlants, Genetically ModifiedTwo-Hybrid System TechniquesUbiquitin-Protein LigasesArabidopsis ProteinsARR10 protein, ArabidopsisCytokininsDNA-Binding ProteinsGTP-Binding ProteinsHeterotrimeric GTP-Binding ProteinsPUB2 protein, ArabidopsisPUB4 protein, ArabidopsisUbiquitin-Protein LigasesXLG1 protein, ArabidopsisXLG2 protein, ArabidopsisXLG3 protein, Arabidopsis

Identifiers

PMID27986866
PMCPMC5291011
OpenAlexW2565884518

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.