Evidence map›Paper›PMID 27208238›Full record

ArticlePlant physiology2016

A Mutation in the Catalytic Subunit of the Glycosylphosphatidylinositol Transamidase Disrupts Growth, Fertility, and Stomata Formation.

Mark G R Bundy, Pawel Z Kosentka, Alaina H Willet, Liang Zhang, Emily Miller, Elena D Shpak

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
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  11. Characterization ofFrontiers in plant science · 2022
    Article
  12. Increasing Expression ofFrontiers in plant science · 2022
    Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. The Temperature-Dependent Retention of Introns inInternational journal of molecular sciences · 2019
    Article
  19. Glycosylphosphatidylinositol-Anchored Proteins inFrontiers in plant science · 2019
    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

6 authors at 1 institution in 1 country.

Mark G R BundyDepartment of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996.ORCID 0000-0002-4463-3382
Pawel Z KosentkaDepartment of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996.ORCID 0000-0001-5009-4488
Alaina H WilletDepartment of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996.ORCID 0000-0002-0163-4772
Liang ZhangDepartment of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996.ORCID 0000-0002-1395-0465
Emily MillerDepartment of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996.ORCID 0000-0001-6956-2253
Elena D ShpakDepartment of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996 shpak@utk.edu.ORCID 0000-0002-5702-7517
University of Tennessee at Knoxville · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

GPI-anchored proteins (GPI-APs) are essential for plant growth and development; knockout mutations in enzymes responsible for anchor biosynthesis or attachment are gametophyte or embryo lethal. In a genetic screen targeted to identify genes regulating stomata formation, we discovered a missense mutation in the Arabidopsis (Arabidopsis thaliana) homolog of GPI8/PIG-K, a Cys protease that transfers an assembled GPI anchor to proteins. The Arabidopsis genome has a single copy of AtGPI8, and the atgpi8-1 mutation reduces the efficiency of this enzyme, leading to reduced accumulation of GPI-anchored proteins. While the atgpi8-1 mutation strongly disrupts plant growth, it is not lethal. Phenotypic analysis of atgpi8-1 mutants suggests that GPI-APs are important for root and shoot growth, stomata formation, apical dominance, transition to flowering, and male gametophyte viability. In addition, atgpi8-1 mutants accumulate higher levels of callose and have reduced plasmodesmata permeability. Genetic interactions of atgpi8-1 with mutations in ERECTA family (ERf) genes suggest the existence of a GPI-AP in a branch of the ERf signaling pathway that regulates stomata formation. Activation of the ERf signal transduction cascade by constitutively active YODA rescues stomata clustering in atgpi8-1, indicating that a GPI-AP functions upstream of the MAP kinase cascade. TOO MANY MOUTHS (TMM) is a receptor-like protein that is able to form heterodimers with ERfs. Our analysis demonstrates that tmm-1 is epistatic to atgpi8-1, indicating that either TMM is a GPI-AP or there is another GPI-AP regulating stomata development whose function is dependent upon TMM.

Indexed as

Amino Acid SequenceAminoacyltransferasesArabidopsisArabidopsis ProteinsCatalytic DomainCysteine ProteasesFertilityGlucansGlycosylphosphatidylinositolsMutationPlant StomataPlasmodesmataPollenSeedlingsSequence AlignmentSignal TransductionAminoacyltransferasesArabidopsis ProteinscalloseCysteine ProteasesGlucansGlycosylphosphatidylinositolstoo many mouths protein, Arabidopsistransamidases

Identifiers

PMID27208238
PMCPMC4902618
OpenAlexW2415114282

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.