Evidence map›Paper›PMID 16183741›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Cysteine protease mcII-Pa executes programmed cell death during plant embryogenesis.

Peter V Bozhkov, Maria F Suarez, Lada H Filonova, Geoffrey Daniel, Andrey A Zamyatnin, Salvador Rodriguez-Nieto, Boris Zhivotovsky, Andrei Smertenko

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

94 citing papers in PubMed, 254 citations in OpenAlex.

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  17. The Role of Pseudo-Orthocaspase (SyOC) ofFrontiers in microbiology · 2021
    Article
  18. Article
  19. Identification and characterization ofBiochemistry and biophysics reports · 2019
    Article
  20. Protein S-nitrosylation in programmed cell death in plants.Cellular and molecular life sciences : CMLS · 2019
    Review

34 more citing papers are in PubMed but not listed here.

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

8 authors at 1 institution in 1 country.

Peter V BozhkovDepartment of Plant Biology and Forest Genetics, Swedish University of Agricultural Sciences, Box 7080, SE-75007 Uppsala, Sweden. peter.bozhkov@vbsg.slu.se
Maria F Suarez
Lada H Filonova
Geoffrey Daniel
Andrey A Zamyatnin
Salvador Rodriguez-Nieto
Boris Zhivotovsky
Andrei Smertenko
Swedish University of Agricultural Sciences · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Programmed cell death (PCD) is indispensable for eukaryotic development. In animals, PCD is executed by the caspase family of cysteine proteases. Plants do not have close homologues of caspases but possess a phylogenetically distant family of cysteine proteases named metacaspases. The cellular function of metacaspases in PCD is unknown. Here we show that during plant embryogenesis, metacaspase mcII-Pa translocates from the cytoplasm to nuclei in terminally differentiated cells that are destined for elimination, where it colocalizes with the nuclear pore complex and chromatin, causing nuclear envelope disassembly and DNA fragmentation. The cell-death function of mcII-Pa relies on its cysteine-dependent arginine-specific proteolytic activity. Accordingly, mutation of catalytic cysteine abrogates the proteolytic activity of mcII-Pa and blocks nuclear degradation. These results establish metacaspase as an executioner of PCD during embryo patterning and provide a functional link between PCD and embryogenesis in plants. Although mcII-Pa and metazoan caspases have different substrate specificity, they serve a common function during development, demonstrating the evolutionary parallelism of PCD pathways in plants and animals.

Indexed as

ApoptosisBase SequenceCell NucleusCysteine EndopeptidasesDNA FragmentationImmunoblottingImmunohistochemistryIn Situ Nick-End LabelingKineticsMicroscopy, ElectronMicroscopy, FluorescenceMolecular Sequence DataPiceaSequence Analysis, DNASubstrate SpecificityCysteine Endopeptidases

Identifiers

PMID16183741
PMCPMC1242326
OpenAlexW2018569292

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.