Evidence map›Paper›PMID 24719325›Full record

ArticleThe Journal of biological chemistry2014

Arabidopsis AtPARK13, which confers thermotolerance, targets misfolded proteins.

Indranil Basak, Ramavati Pal, Ketan S Patil, Aisling Dunne, Hsin-Pin Ho, Sungsu Lee, Diluka Peiris, Jodi Maple-Grødem, Mark Odell, Emmanuel J Chang and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

12 citing papers in PubMed, 25 citations in OpenAlex.

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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

12 authors at 4 institutions in 3 countries.

Indranil BasakFrom the Department of Biological Sciences, St. John's University, New York, New York 11439.
Ramavati PalFrom the Department of Biological Sciences, St. John's University, New York, New York 11439.
Ketan S PatilFrom the Department of Biological Sciences, St. John's University, New York, New York 11439.
Aisling DunneFrom the Department of Biological Sciences, St. John's University, New York, New York 11439.
Hsin-Pin Hothe Department of Chemistry, York College of the City University of New York, New York, New York 11451.
Sungsu LeeFrom the Department of Biological Sciences, St. John's University, New York, New York 11439.
Diluka Peiristhe Department of Molecular and Applied Biosciences, University of Westminster, London W1W 6UW, United Kingdom, and.
Jodi Maple-Grødemthe Norwegian Center for Movement Disorders, Stavanger University Hospital, 4068 Stavanger, Norway.
Mark Odellthe Department of Molecular and Applied Biosciences, University of Westminster, London W1W 6UW, United Kingdom, and.
Emmanuel J Changthe Department of Chemistry, York College of the City University of New York, New York, New York 11451.
Jan Petter Larsenthe Norwegian Center for Movement Disorders, Stavanger University Hospital, 4068 Stavanger, Norway.
Simon G MøllerFrom the Department of Biological Sciences, St. John's University, New York, New York 11439, the Norwegian Center for Movement Disorders, Stavanger University Hospital, 4068 Stavanger, Norway mollers@stjohns.edu.
St. John's University · USStavanger University Hospital · NOUniversity of Westminster · GBYork College, City University of New York · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mutations in HTRA2/Omi/PARK13 have been implicated in Parkinson disease (PD). PARK13 is a neuroprotective serine protease; however, little is known about how PARK13 confers stress protection and which protein targets are directly affected by PARK13. We have reported that Arabidopsis thaliana represents a complementary PD model, and here we demonstrate that AtPARK13, similar to human PARK13 (hPARK13), is a mitochondrial protease. We show that the expression/accumulation of AtPARK13 transcripts are induced by heat stress but not by other stress conditions, including oxidative stress and metals. Our data show that elevated levels of AtPARK13 confer thermotolerance in A. thaliana. Increased temperatures accelerate protein unfolding, and we demonstrate that although AtPARK13 can act on native protein substrates, unfolded proteins represent better AtPARK13 substrates. The results further show that AtPARK13 and hPARK13 can degrade the PD proteins α-synuclein (SNCA) and DJ-1/PARK7 directly, without autophagy involvement, and that misfolded SNCA and DJ-1 represent better substrates than their native counterparts. Comparative proteomic profiling revealed AtPARK13-mediated proteome changes, and we identified four proteins that show altered abundance in response to AtPARK13 overexpression and elevated temperatures. Our study not only suggests that AtPARK13 confers thermotolerance by degrading misfolded protein targets, but it also provides new insight into possible roles of this protease in neurodegeneration.

Indexed as

Hot TemperatureAdaptation, Physiologicalalpha-SynucleinAmino Acid SequenceArabidopsisArabidopsis ProteinsBlotting, WesternCloning, MolecularGene Expression ProfilingHumansIntracellular Signaling Peptides and ProteinsKineticsLuminescent ProteinsMicroscopy, ConfocalMitochondriaMitochondrial Proteinsalpha-SynucleinArabidopsis ProteinsIntracellular Signaling Peptides and ProteinsLuminescent ProteinsMitochondrial ProteinsOncogene ProteinsPARK13 protein, ArabidopsisPARK7 protein, humanPeptide HydrolasesProtein Deglycase DJ-1Serine ProteasesArabidopsisHeat StressParkinson DiseaseProteaseProteomicsStress

Identifiers

PMID24719325
PMCPMC4031502
OpenAlexW2056831906

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.