Evidence map›Paper›PMID 26463087›Full record

ArticlePlant physiology2015

Phosphatase and Tensin Homolog Is a Growth Repressor of Both Rhizoid and Gametophore Development in the Moss Physcomitrella patens.

Laura Saavedra, Rita Catarino, Tobias Heinz, Ingo Heilmann, Magdalena Bezanilla, Rui Malhó

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed, 1 pooled it
0.9field-weighted citation impact, top 25% 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, 1 synthesis or guideline pooled it, 20 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  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

6 authors at 3 institutions in 3 countries.

Laura SaavedraUniversidade de Lisboa, Faculdade de Ciências, Biosystems and Integrative Sciences Institute, Campo Grande, 1749-016 Lisboa, Portugal (L.S., R.C., R.M.);Institute of Biochemistry and Biotechnology/Cellular Biochemistry, Martin-Luther-University Halle-Wittenberg, 06120 Halle, Germany (T.H., I.H.); andUniversity of Massachusetts, Amherst, Massachusetts 01003 (M.B.) laura.saavedra@conicet.gov.ar r.malho@fc.ul.pt.
Rita CatarinoUniversidade de Lisboa, Faculdade de Ciências, Biosystems and Integrative Sciences Institute, Campo Grande, 1749-016 Lisboa, Portugal (L.S., R.C., R.M.);Institute of Biochemistry and Biotechnology/Cellular Biochemistry, Martin-Luther-University Halle-Wittenberg, 06120 Halle, Germany (T.H., I.H.); andUniversity of Massachusetts, Amherst, Massachusetts 01003 (M.B.).ORCID http://orcid.org/0000-0002-2638-0334
Tobias HeinzUniversidade de Lisboa, Faculdade de Ciências, Biosystems and Integrative Sciences Institute, Campo Grande, 1749-016 Lisboa, Portugal (L.S., R.C., R.M.);Institute of Biochemistry and Biotechnology/Cellular Biochemistry, Martin-Luther-University Halle-Wittenberg, 06120 Halle, Germany (T.H., I.H.); andUniversity of Massachusetts, Amherst, Massachusetts 01003 (M.B.).ORCID http://orcid.org/0000-0002-8052-0932
Ingo HeilmannUniversidade de Lisboa, Faculdade de Ciências, Biosystems and Integrative Sciences Institute, Campo Grande, 1749-016 Lisboa, Portugal (L.S., R.C., R.M.);Institute of Biochemistry and Biotechnology/Cellular Biochemistry, Martin-Luther-University Halle-Wittenberg, 06120 Halle, Germany (T.H., I.H.); andUniversity of Massachusetts, Amherst, Massachusetts 01003 (M.B.).
Magdalena BezanillaUniversidade de Lisboa, Faculdade de Ciências, Biosystems and Integrative Sciences Institute, Campo Grande, 1749-016 Lisboa, Portugal (L.S., R.C., R.M.);Institute of Biochemistry and Biotechnology/Cellular Biochemistry, Martin-Luther-University Halle-Wittenberg, 06120 Halle, Germany (T.H., I.H.); andUniversity of Massachusetts, Amherst, Massachusetts 01003 (M.B.).ORCID http://orcid.org/0000-0001-6124-9916
Rui MalhóUniversidade de Lisboa, Faculdade de Ciências, Biosystems and Integrative Sciences Institute, Campo Grande, 1749-016 Lisboa, Portugal (L.S., R.C., R.M.);Institute of Biochemistry and Biotechnology/Cellular Biochemistry, Martin-Luther-University Halle-Wittenberg, 06120 Halle, Germany (T.H., I.H.); andUniversity of Massachusetts, Amherst, Massachusetts 01003 (M.B.) laura.saavedra@conicet.gov.ar r.malho@fc.ul.pt.ORCID http://orcid.org/0000-0001-5287-869X
University of Lisbon · PTMartin Luther University Halle-Wittenberg · DEUniversity of Massachusetts Amherst · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphatase and tensin homolog deleted on chromosome 10 (PTEN) is a lipid phosphatase implicated in cellular proliferation and survival. In animal cells, loss of PTEN leads to increased levels of phosphatidylinositol (3,4,5)-trisphosphate, stimulation of glucose and lipid metabolism, cellular growth, and morphological changes (related to adaptation and survival). Intriguingly, in plants, phosphatidylinositol (3,4,5)-trisphosphate has not been detected, and the enzymes that synthesize it were never reported. In this study we performed a genetic, biochemical, and functional characterization of the moss Physcomitrella patens PTEN gene family. P. patens has four PTENs, which are ubiquitously expressed during the entire moss life cycle. Using a knock-in approach, we show that all four genes are expressed in growing tissues, namely caulonemal and rhizoid cells. At the subcellular level, PpPTEN-green fluorescent protein fusions localized to the cytosol and the nucleus. Analysis of single and double knockouts revealed no significant phenotypes at different developmental stages, indicative of functional redundancy. However, compared with wild-type triple and quadruple pten knockouts, caulonemal cells grew faster, switched from the juvenile protonemal stage to adult gametophores earlier, and produced more rhizoids. Furthermore, analysis of lipid content and quantitative real-time polymerase chain reaction data performed in quadruple mutants revealed altered phosphoinositide levels [increase in phosphatidylinositol (3,5)-bisphosphate and decrease in phosphatidylinositol 3-phosphate] and up-regulation of marker genes from the synthesis phase of the cell cycle (e.g. P. patens proliferating cell nuclear antigen, ribonucleotide reductase, and minichromosome maintenance) and of the retinoblastoma-related protein gene P. patens retinoblastoma-related protein1. Together, these results suggest that PpPTEN is a suppressor of cell growth and morphogenic development in plants.

Indexed as

Gene Expression Regulation, PlantAmino Acid SequenceBryopsidaCell CycleGene Knockout TechniquesMicrofilament ProteinsMutationPhenotypePhosphatidylinositol PhosphatesPlant ProteinsPTEN PhosphohydrolaseSequence AlignmentTensinsUp-RegulationMicrofilament Proteinsphosphatidylinositol 3-phosphatePhosphatidylinositol PhosphatesPlant ProteinsPTEN PhosphohydrolaseTensins

Identifiers

PMID26463087
PMCPMC4677911
OpenAlexW2125771051

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.