Evidence map›Paper›PMID 27923987›Full record

ArticlePlant physiology2017

Activation of Mitochondrial Protein Phosphatase SLP2 by MIA40 Regulates Seed Germination.

R Glen Uhrig, Anne-Marie Labandera, Lay-Yin Tang, Nicolas A Sieben, Marilyn Goudreault, Edward Yeung, Anne-Claude Gingras, Marcus A Samuel, Greg B G Moorhead

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
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 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

9 citing papers in PubMed, 26 citations in OpenAlex.

  1. Oxidation ofAntioxidants (Basel, Switzerland) · 2023
    Article
  2. mSphere · 2022
    Article
  3. Article
  4. Review
  5. Retrograde signals from mitochondria reprogramme skoto-morphogenesis inPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020
    Article
  6. Targeted Profiling ofThe Plant cell · 2018
    Article
  7. Review
  8. Article
  9. 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

9 authors at 2 institutions in 3 countries.

R Glen UhrigDepartment of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada (R.G.U., A.-M.L.,L.-Y.T., N.A.S., E.Y., M.A.S., G.B.G.M.); moorhead@ucalgary.ca.ORCID 0000-0003-2773-4381
Anne-Marie LabanderaDepartment of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada (R.G.U., A.-M.L.,L.-Y.T., N.A.S., E.Y., M.A.S., G.B.G.M.).ORCID 0000-0002-0593-4166
Lay-Yin TangDepartment of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada (R.G.U., A.-M.L.,L.-Y.T., N.A.S., E.Y., M.A.S., G.B.G.M.).
Nicolas A SiebenDepartment of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada (R.G.U., A.-M.L.,L.-Y.T., N.A.S., E.Y., M.A.S., G.B.G.M.).ORCID 0000-0002-7981-7827
Marilyn GoudreaultDepartment of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada (R.G.U., A.-M.L.,L.-Y.T., N.A.S., E.Y., M.A.S., G.B.G.M.).
Edward YeungDepartment of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada (R.G.U., A.-M.L.,L.-Y.T., N.A.S., E.Y., M.A.S., G.B.G.M.).
Anne-Claude GingrasDepartment of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada (R.G.U., A.-M.L.,L.-Y.T., N.A.S., E.Y., M.A.S., G.B.G.M.).
Marcus A SamuelDepartment of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada (R.G.U., A.-M.L.,L.-Y.T., N.A.S., E.Y., M.A.S., G.B.G.M.).
Greg B G MoorheadDepartment of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada (R.G.U., A.-M.L.,L.-Y.T., N.A.S., E.Y., M.A.S., G.B.G.M.); moorhead@ucalgary.ca.ORCID 0000-0003-3282-7590
Mount Sinai Hospital · CAUniversity of Calgary · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reversible protein phosphorylation catalyzed by protein kinases and phosphatases represents the most prolific and well-characterized posttranslational modification known. Here, we demonstrate that Arabidopsis (Arabidopsis thaliana) Shewanella-like protein phosphatase 2 (AtSLP2) is a bona fide Ser/Thr protein phosphatase that is targeted to the mitochondrial intermembrane space (IMS) where it interacts with the mitochondrial oxidoreductase import and assembly protein 40 (AtMIA40), forming a protein complex. Interaction with AtMIA40 is necessary for the phosphatase activity of AtSLP2 and is dependent on the formation of disulfide bridges on AtSLP2. Furthermore, by utilizing atslp2 null mutant, AtSLP2 complemented and AtSLP2 overexpressing plants, we identify a function for the AtSLP2-AtMIA40 complex in negatively regulating gibberellic acid-related processes during seed germination. Results presented here characterize a mitochondrial IMS-localized protein phosphatase identified in photosynthetic eukaryotes as well as a protein phosphatase target of the highly conserved eukaryotic MIA40 IMS oxidoreductase.

Indexed as

GerminationAbscisic AcidAmino Acid SequenceArabidopsisArabidopsis ProteinsBiosynthetic PathwaysDisulfidesEnzyme ActivationGibberellinsMitochondriaMitochondrial MembranesMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsModels, BiologicalOxidation-ReductionProtein BindingAbscisic AcidArabidopsis ProteinsDisulfidesgibberellic acidGibberellinsMia40 protein, ArabidopsisMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsSLP2 protein, ArabidopsisTriazolesuniconazole

Identifiers

PMID27923987
PMCPMC5291043
OpenAlexW2560815881

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.