Evidence map›Paper›PMID 31818884›Full record

ArticleLife science alliance2020

MERLIN: a novel BRET-based proximity biosensor for studying mitochondria-ER contact sites.

Vanessa Hertlein, Hector Flores-Romero, Kushal K Das, Sebastian Fischer, Michael Heunemann, Maria Calleja-Felipe, Shira Knafo, Katharina Hipp, Klaus Harter, Julia C Fitzgerald and 1 more

Abstract read
In one paragraph

Article in Life science alliance, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
–field-weighted citation impact
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

33 citing papers in PubMed.

  1. Review
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  5. MTCH2 promotes BAX and BAK self-assembly and apoptotic pore growth.Nature structural & molecular biology · 2026
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  8. Review
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  15. Imaging interorganelle contacts at a glance.Journal of cell science · 2024
    Review
  16. Article
  17. Review
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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

11 authors.

Vanessa HertleinInterfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.ORCID 0000-0003-4476-6748
Hector Flores-RomeroInterfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.ORCID 0000-0003-0996-5717
Kushal K DasInterfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.
Sebastian FischerUniversity of Heidelberg, Heidelberg, Germany.
Michael HeunemannCenter for Plant Molecular Biology, University of Tübingen, Tübingen, Germany.
Maria Calleja-FelipeMolecular Cognition Laboratory, Biophysics Institute, Consejo Superior de Investigaciones Cientificas, University of the Basque Country (UPV)/Euskal Herriko University, Campus Universidad del País Vasco, Leioa, Spain.ORCID 0000-0002-8374-3867
Shira KnafoMolecular Cognition Laboratory, Biophysics Institute, Consejo Superior de Investigaciones Cientificas, University of the Basque Country (UPV)/Euskal Herriko University, Campus Universidad del País Vasco, Leioa, Spain.
Katharina HippMax Planck Institute for Developmental Biology, Tübingen, Germany.ORCID 0000-0002-1493-9698
Klaus HarterCenter for Plant Molecular Biology, University of Tübingen, Tübingen, Germany.
Julia C FitzgeraldHertie-Institute for Clinical Brain Research, University of Tübingen and German Centre for Neurodegenerative Diseases (DZNE), Tübingen, Germany.
Ana J García-SáezInterfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany ana.garcia@uni-koeln.de.ORCID 0000-0002-3894-5945

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The contacts between the ER and mitochondria play a key role in cellular functions such as the exchange of lipids and calcium between both organelles, as well as in apoptosis and autophagy signaling. The molecular architecture and spatiotemporal regulation of these distinct contact regions remain obscure and there is a need for new tools that enable tackling these questions. Here, we present a new bioluminescence resonance energy transfer-based biosensor for the quantitative analysis of distances between the ER and mitochondria that we call MERLIN (Mitochondria-ER Length Indicator Nanosensor). The main advantages of MERLIN compared with available alternatives are that it does not rely on the formation of artificial physical links between the two organelles, which could lead to artifacts, and that it allows to study contact site reversibility and dynamics. We show the applicability of MERLIN by characterizing the role of the mitochondrial dynamics machinery on the contacts of this organelle with the ER.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsApoptosisBioluminescence Resonance Energy Transfer TechniquesBiosensing TechniquesChlorocebus aethiopsDynaminsEndoplasmic ReticulumGene Knockdown TechniquesGTP PhosphohydrolasesHCT116 CellsHumansMiceMitochondriaMitochondrial DynamicsMitochondrial MembranesAdaptor Proteins, Signal TransducingDNM1L protein, humanDynaminsGTP PhosphohydrolasesMfn1 protein, humanMFN2 protein, humanMitochondrial Membrane Transport ProteinsMitochondrial ProteinsPDZD8 protein, human

Identifiers

PMID31818884
PMCPMC6910062

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Registered trials

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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.