Evidence map›Paper›PMID 29434276›Full record

ArticleScientific reports2018

The Extracellular Domain of Pollen Receptor Kinase 3 is structurally similar to the SERK family of co-receptors.

Sayan Chakraborty, Haiyun Pan, Qingyu Tang, Colin Woolard, Guozhou Xu

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

8 citing papers in PubMed, 12 citations in OpenAlex.

  1. First EST-SSRs ofPlants (Basel, Switzerland) · 2025
    Article
  2. Article
  3. Genome-wide association study for candidate genes controlling seed yield and its components in rapeseed (Physiology and molecular biology of plants : an international journal of functional plant biology · 2021
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. 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.

Sayan ChakrabortyDepartment of Molecular and Structural Biochemistry, North Carolina State University, 128 Polk Hall, Raleigh, 27695, USA.ORCID 0000-0002-2580-5097
Haiyun PanDepartment of Molecular and Structural Biochemistry, North Carolina State University, 128 Polk Hall, Raleigh, 27695, USA.
Qingyu TangDepartment of Molecular and Structural Biochemistry, North Carolina State University, 128 Polk Hall, Raleigh, 27695, USA.
Colin WoolardDepartment of Molecular and Structural Biochemistry, North Carolina State University, 128 Polk Hall, Raleigh, 27695, USA.
Guozhou XuDepartment of Molecular and Structural Biochemistry, North Carolina State University, 128 Polk Hall, Raleigh, 27695, USA. gxu3@ncsu.edu.ORCID 0000-0003-4939-5982
North Carolina State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During reproduction in flowering plants, the male gametophyte delivers an immotile male gamete to the female gametophyte in the pistil by formation of pollen tubes. In Arabidopsis thaliana, two synergid cells situated on either side of the egg cell produce cysteine-rich chemoattractant peptide LURE that guides the pollen tube to the female gametophyte for sexual reproduction. Recently, in Arabidopsis thaliana, Pollen Receptor Kinase 3 (PRK3), along with PRK1, PRK6, and PRK8, have been predicted to be the receptors responsible for sensing LURE. These receptors belong to the Leucine Rich Repeat Receptor Like Kinases (LRR-RLKs), the largest family of receptor kinases found in Arabidopsis thaliana. How PRKs regulate the growth and development of the pollen tube remains elusive. In order to better understand the PRK-mediated signaling mechanism in pollen tube growth and guidance, we have determined the crystal structure of the extracellular domain (ecd) of PRK3 at 2.5 Å, which resembles the SERK family of plant co-receptors. The structure of ecdPRK3 is composed of a conserved surface that coincides with the conserved receptor-binding surface of the SERK family of co-receptors. Our structural analyses of PRK3 have provided a template for future functional studies of the PRK family of LRR-RLK receptors in the regulation of pollen tube development.

Indexed as

ArabidopsisArabidopsis ProteinsFlowersOvulePlant ProteinsPollenPollen TubePollinationProtein KinasesProtein Serine-Threonine KinasesReproductionSignal TransductionArabidopsis ProteinsPlant ProteinsPRK1 protein, ArabidopsisPRK3 protein, ArabidopsisPRK6 protein, ArabidopsisPRK8 protein, ArabidopsisProtein KinasesProtein Serine-Threonine KinasesSERK protein, plant

Identifiers

PMID29434276
PMCPMC5809528
OpenAlexW2806816105

What OpenQuestion holds

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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.