Evidence map›Paper›PMID 28628643›Full record

ArticlePloS one2017

Mis-targeting of the mitochondrial protein LIPT2 leads to apoptotic cell death.

Emanuele Bernardinelli, Roberta Costa, Giada Scantamburlo, Janet To, Rossana Morabito, Charity Nofziger, Carolina Doerrier, Gerhard Krumschnabel, Markus Paulmichl, Silvia Dossena

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.2field-weighted citation impact, top 44% 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

11 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
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  11. Protein moonlighting elucidates the essential human pathway catalyzing lipoic acid assembly on its cognate enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2018
    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 5 institutions in 3 countries.

Emanuele BernardinelliInstitute of Pharmacology and Toxicology, Paracelsus Medical University, Salzburg, Austria.
Roberta CostaInstitute of Pharmacology and Toxicology, Paracelsus Medical University, Salzburg, Austria.
Giada ScantamburloInstitute of Pharmacology and Toxicology, Paracelsus Medical University, Salzburg, Austria.
Janet ToSchool of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
Rossana MorabitoDepartment of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina, Messina, Italy.
Charity NofzigerInstitute of Pharmacology and Toxicology, Paracelsus Medical University, Salzburg, Austria.
Carolina DoerrierOroboros Instruments, Innsbruck, Austria.
Gerhard KrumschnabelOroboros Instruments, Innsbruck, Austria.
Markus PaulmichlCenter for Health and Bioresources, Austrian Institute of Technology, Vienna, Austria.
Silvia DossenaInstitute of Pharmacology and Toxicology, Paracelsus Medical University, Salzburg, Austria.ORCID http://orcid.org/0000-0002-6694-9249
Paracelsus Medical University · ATOroboros Instruments (Austria) · ATAustrian Institute of Technology · ATNanyang Technological University · SGUniversity of Messina · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipoyl(Octanoyl) Transferase 2 (LIPT2) is a protein involved in the post-translational modification of key energy metabolism enzymes in humans. Defects of lipoic acid synthesis and transfer start to emerge as causes of fatal or severe early-onset disease. We show that the first 31 amino acids of the N-terminus of LIPT2 represent a mitochondrial targeting sequence and inhibition of the transit of LIPT2 to the mitochondrion results in apoptotic cell death associated with activation of the apoptotic volume decrease (AVD) current in normotonic conditions, as well as over-activation of the swelling-activated chloride current (IClswell), mitochondrial membrane potential collapse, caspase-3 cleavage and nuclear DNA fragmentation. The findings presented here may help elucidate the molecular mechanisms underlying derangements of lipoic acid biosynthesis.

Indexed as

ApoptosisAcyltransferasesCalreticulinCaspase 3ChloridesDNA FragmentationHEK293 CellsHeLa CellsHumansMembrane Potential, MitochondrialMicroscopy, ConfocalMitochondriaPatch-Clamp TechniquesPlasmidsRNA InterferenceRNA, Small InterferingAcyltransferasesCalreticulinCaspase 3Chlorideslipoyltransferase IIRNA, Small InterferingStaurosporineThioctic Acid

Identifiers

PMID28628643
PMCPMC5476274
OpenAlexW2696357186

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.