Evidence map›Paper›PMID 16698944›Full record

ArticleThe Plant cell2006

Arabidopsis PASTICCINO2 is an antiphosphatase involved in regulation of cyclin-dependent kinase A.

Marco Da Costa, Liên Bach, Isabelle Landrieu, Yannick Bellec, Olivier Catrice, Spencer Brown, Lieven De Veylder, Guy Lippens, Dirk Inzé, Jean-Denis Faure

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
7.5field-weighted citation impact, top 3% 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

18 citing papers in PubMed, 61 citations in OpenAlex.

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  9. Extensive changes to alternative splicing patterns following allopolyploidy in natural and resynthesized polyploids.Proceedings of the National Academy of Sciences of the United States of America · 2011
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  10. Review
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  17. The very-long-chain hydroxy fatty acyl-CoA dehydratase PASTICCINO2 is essential and limiting for plant development.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  18. 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

10 authors at 6 institutions in 2 countries.

Marco Da CostaLaboratoire de Biologie Cellulaire, Institut National de la Recherche Agronomique, F-78026 Versailles Cedex, France.
Liên Bach
Isabelle Landrieu
Yannick Bellec
Olivier Catrice
Spencer Brown
Lieven De Veylder
Guy Lippens
Dirk Inzé
Jean-Denis Faure
Laboratoire de Génétique Cellulaire · FRInstitut des Sciences du Végétal · FRGhent University · BEInstitut Pasteur de Lille · FRUniversité de Lille · FRVlaams Instituut voor Biotechnologie · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PASTICCINO2 (PAS2), a member of the protein Tyr phosphatase-like family, is conserved among all eukaryotes and is characterized by a mutated catalytic site. The cellular functions of the Tyr phosphatase-like proteins are still unknown, even if they are essential in yeast and mammals. Here, we demonstrate that PAS2 interacts with a cyclin-dependent kinase (CDK) that is phosphorylated on Tyr and not with its unphosphorylated isoform. Phosphorylation of the conserved regulatory Tyr-15 is involved in the binding of CDK to PAS2. Loss of the PAS2 function dephosphorylated Arabidopsis thaliana CDKA;1 and upregulated its kinase activity. In accordance with its role as a negative regulator of the cell cycle, overexpression of PAS2 slowed down cell division in suspension cell cultures at the G2-to-M transition and early mitosis and inhibited Arabidopsis seedling growth. The latter was accompanied by altered leaf development and accelerated cotyledon senescence. PAS2 was localized in the cytoplasm of dividing cells but moved into the nucleus upon cell differentiation, suggesting that the balance between cell division and differentiation is regulated through the interaction between CDKA;1 and the antiphosphatase PAS2.

Indexed as

Gene Expression Regulation, PlantArabidopsisArabidopsis ProteinsCell DivisionCyclin-Dependent KinasesGene ExpressionModels, BiologicalMolecular Sequence DataNicotianaPhosphoric Monoester HydrolasesPhosphorylationProtein BindingSubcellular FractionsArabidopsis ProteinsCDKA1 protein, ArabidopsisCyclin-Dependent KinasesPEPINO protein, ArabidopsisPhosphoric Monoester Hydrolases

Identifiers

PMID16698944
PMCPMC1475488
OpenAlexW2162101893

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.