Evidence map›Paper›PMID 27506240›Full record

ArticlePlant physiology2016

The DEK1 Calpain Linker Functions in Three-Dimensional Body Patterning in Physcomitrella patens.

Wenche Johansen, Ako Eugene Ako, Viktor Demko, Pierre-François Perroud, Stephan A Rensing, Ahmed Khaleel Mekhlif, Odd-Arne Olsen

Open access · bronzeAbstract 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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.2field-weighted citation impact, top 19% 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

16 citing papers in PubMed, 31 citations in OpenAlex.

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  7. microPublication biology · 2023
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  11. Review
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  13. International journal of molecular sciences · 2021
    Review
  14. Challenges ofPlant signaling & behavior · 2020
    Article
  15. Article
  16. 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

7 authors at 2 institutions in 2 countries.

Wenche JohansenHedmark University of Applied Sciences, N-2418 Elverum, Norway (W.J., A.E.A., A.K.M.);Norwegian University of Life Sciences, N-1432 Aas, Norway (V.D., O.-A.O.); andPhilipps University Marburg, Plant Cell Biology, 35043 Marburg, Germany (P.-F.P., S.A.R.) wenche.johansen@hihm.no odd-arne.olsen@nmbu.no.ORCID 0000-0002-9240-586X
Ako Eugene AkoHedmark University of Applied Sciences, N-2418 Elverum, Norway (W.J., A.E.A., A.K.M.);Norwegian University of Life Sciences, N-1432 Aas, Norway (V.D., O.-A.O.); andPhilipps University Marburg, Plant Cell Biology, 35043 Marburg, Germany (P.-F.P., S.A.R.).ORCID 0000-0002-1402-5861
Viktor DemkoHedmark University of Applied Sciences, N-2418 Elverum, Norway (W.J., A.E.A., A.K.M.);Norwegian University of Life Sciences, N-1432 Aas, Norway (V.D., O.-A.O.); andPhilipps University Marburg, Plant Cell Biology, 35043 Marburg, Germany (P.-F.P., S.A.R.).
Pierre-François PerroudHedmark University of Applied Sciences, N-2418 Elverum, Norway (W.J., A.E.A., A.K.M.);Norwegian University of Life Sciences, N-1432 Aas, Norway (V.D., O.-A.O.); andPhilipps University Marburg, Plant Cell Biology, 35043 Marburg, Germany (P.-F.P., S.A.R.).ORCID 0000-0001-7607-3618
Stephan A RensingHedmark University of Applied Sciences, N-2418 Elverum, Norway (W.J., A.E.A., A.K.M.);Norwegian University of Life Sciences, N-1432 Aas, Norway (V.D., O.-A.O.); andPhilipps University Marburg, Plant Cell Biology, 35043 Marburg, Germany (P.-F.P., S.A.R.).ORCID 0000-0002-0225-873X
Ahmed Khaleel MekhlifHedmark University of Applied Sciences, N-2418 Elverum, Norway (W.J., A.E.A., A.K.M.);Norwegian University of Life Sciences, N-1432 Aas, Norway (V.D., O.-A.O.); andPhilipps University Marburg, Plant Cell Biology, 35043 Marburg, Germany (P.-F.P., S.A.R.).
Odd-Arne OlsenHedmark University of Applied Sciences, N-2418 Elverum, Norway (W.J., A.E.A., A.K.M.);Norwegian University of Life Sciences, N-1432 Aas, Norway (V.D., O.-A.O.); andPhilipps University Marburg, Plant Cell Biology, 35043 Marburg, Germany (P.-F.P., S.A.R.) wenche.johansen@hihm.no odd-arne.olsen@nmbu.no.ORCID 0000-0002-8787-1057
Norwegian University of Life Sciences · NOPhilipps University of Marburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The DEFECTIVE KERNEL1 (DEK1) calpain is a conserved 240-kD key regulator of three-dimensional body patterning in land plants acting via mitotic cell plane positioning. The activity of the cytosolic C-terminal calpain protease is regulated by the membrane-anchored DEK1 MEM, which is connected to the calpain via the 600-amino acid residue Linker. Similar to the calpain and MEM domains, the Linker is highly conserved in the land plant lineage, the similarity dropping sharply compared with orthologous charophyte sequences. Using site-directed mutagenesis, we studied the effect on Physcomitrella patens development by deleting the Linker and two conserved Linker motifs. The results show that removal of the Linker has nearly the same effect as removal of the entire DEK1 gene. In contrast, deletion of the conserved Laminin_G3 (LG3) domain had a milder effect, perturbing leafy gametophore patterning and archegonia development. The LG3 domain from Marchantia polymorpha is fully functional in P. patens, whereas angiosperm sequences are not functional. Deletion of a C-terminal Linker subsegment containing a potential calpain autolytic site severely disturbs gametophore development. Finally, changing one of the three calpain active-site amino acid residues results in the same phenotype as deleting the entire DEK1 gene. Based on the conserved nature of animal and DEK1 calpains, we propose that the DEK1 MEM-Linker complex inactivates the calpain by forcing apart the two calpain subunits carrying the three amino acids of the active site.

Indexed as

MutationAmino Acid MotifsAmino Acid SequenceBinding SitesBryopsidaCalpainCatalytic DomainCell MembraneGene Expression Regulation, DevelopmentalGene Expression Regulation, PlantGenetic Complementation TestModels, MolecularMutagenesis, Site-DirectedPhenotypePlant LeavesPlant ProteinsCalpainPlant Proteins

Identifiers

PMID27506240
PMCPMC5047102
OpenAlexW2519080786

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.