Evidence map›Paper›PMID 22353864›Full record

ArticlePlant signaling & behavior2012

Moonlighting kinases with guanylate cyclase activity can tune regulatory signal networks.

Helen R Irving, Lusisizwe Kwezi, Janet Wheeler, Chris Gehring

Open access · bronzeAbstract read
In one paragraph

Article in Plant signaling & behavior, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
4.4field-weighted citation impact, top 6% 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

21 citing papers in PubMed, 53 citations in OpenAlex.

  1. Abscisic acid binds to anFrontiers in plant science · 2026
    Article
  2. Guanylate cyclase activity in moss: revisiting the role of ERECTA-like receptors.Physiology and molecular biology of plants : an international journal of functional plant biology · 2025
    Article
  3. Review
  4. Review
  5. Article
  6. Moonlighting Proteins Shine New Light on Molecular Signaling Niches.International journal of molecular sciences · 2021
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. New Perspectives on Plant Adenylyl Cyclases.Frontiers in molecular biosciences · 2019
    Article
  13. PlantMP: a database for moonlighting plant proteins.Database : the journal of biological databases and curation · 2019
    Article
  14. Article
  15. Downstream Targets of Cyclic Nucleotides in Plants.Frontiers in plant science · 2018
    Article
  16. Discovery of Novel Functional Centers With Rationally Designed Amino Acid Motifs.Computational and structural biotechnology journal · 2018
    Review
  17. Review
  18. Review
  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

4 authors at 3 institutions in 4 countries.

Helen R IrvingMonash Institute of Pharmaceutical Sciences, Monash University, Parkville, Australia. helen.irving@monash.edu
Lusisizwe Kwezi
Janet Wheeler
Chris Gehring
Monash University · AUDivision of Chemistry · USNorth-West University · ZA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Guanylate cyclase (GC) catalyzes the formation of cGMP and it is only recently that such enzymes have been characterized in plants. One family of plant GCs contains the GC catalytic center encapsulated within the intracellular kinase domain of leucine rich repeat receptor like kinases such as the phytosulfokine and brassinosteroid receptors. In vitro studies show that both the kinase and GC domain have catalytic activity indicating that these kinase-GCs are examples of moonlighting proteins with dual catalytic function. The natural ligands for both receptors increase intracellular cGMP levels in isolated mesophyll protoplast assays suggesting that the GC activity is functionally relevant. cGMP production may have an autoregulatory role on receptor kinase activity and / or contribute to downstream cell expansion responses. We postulate that the receptors are members of a novel class of receptor kinases that contain functional moonlighting GC domains essential for complex signaling roles.

Indexed as

ArabidopsisArabidopsis ProteinsCatalysisCyclic GMPGuanylate CyclasePhosphotransferasesSignal TransductionArabidopsis ProteinsCyclic GMPGuanylate CyclasePhosphotransferases

Identifiers

PMID22353864
PMCPMC3405710
OpenAlexW2027326530

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.