Evidence map›Paper›PMID 33296386›Full record

ArticlePloS one2020

Structures of three MORN repeat proteins and a re-evaluation of the proposed lipid-binding properties of MORN repeats.

Sara Sajko, Irina Grishkovskaya, Julius Kostan, Melissa Graewert, Kim Setiawan, Linda Trübestein, Korbinian Niedermüller, Charlotte Gehin, Antonio Sponga, Martin Puchinger and 6 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2020. 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
2.5field-weighted citation impact, top 9% 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, 20 citations in OpenAlex.

  1. Review
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  7. Review
  8. Structures of the junctophilin/voltage-gated calcium channel interface reveal hot spot for cardiomyopathy mutations.Proceedings of the National Academy of Sciences of the United States of America · 2022
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  13. Distinct architecture and composition of mouse axonemal radial spoke head revealed by cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. To the Surface and Back: Exo- and Endocytic Pathways inFrontiers in cell and developmental biology · 2021
    Review
  15. Targeting JP2: A New Treatment for Pulmonary Hypertension.Oxidative medicine and cellular longevity · 2021
    Review
  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

16 authors at 5 institutions in 5 countries.

Sara SajkoDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Vienna, Austria.ORCID 0000-0002-2563-8786
Irina GrishkovskayaDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Vienna, Austria.
Julius KostanDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Vienna, Austria.
Melissa GraewertEuropean Molecular Biology Laboratory, Hamburg Unit, Hamburg, Germany.
Kim SetiawanDepartment of Cell and Developmental Biology, Biocenter, University of Würzburg, Würzburg, Germany.
Linda TrübesteinDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Vienna, Austria.
Korbinian NiedermüllerDepartment of Cell and Developmental Biology, Biocenter, University of Würzburg, Würzburg, Germany.
Charlotte GehinEuropean Molecular Biology Laboratory, Heidelberg Unit, Heidelberg, Germany.
Antonio SpongaDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Vienna, Austria.
Martin PuchingerDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Vienna, Austria.
Anne-Claude GavinEuropean Molecular Biology Laboratory, Heidelberg Unit, Heidelberg, Germany.
Thomas A LeonardDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Vienna, Austria.
Dimitri I SvergunEuropean Molecular Biology Laboratory, Hamburg Unit, Hamburg, Germany.
Terry K SmithSchool of Biology, BSRC, University of St. Andrews, St. Andrews, United Kingdom.
Brooke MorriswoodDepartment of Cell and Developmental Biology, Biocenter, University of Würzburg, Würzburg, Germany.ORCID 0000-0001-7031-3801
Kristina Djinovic-CarugoDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Vienna, Austria.
University of Vienna · ATEuropean Molecular Biology Laboratory · DEUniversity of Würzburg · DEUniversity of Geneva · CHUniversity of St Andrews · GB

Funding

Austrian Science Fund FWF I 1593Austrian Science Fund FWF I 525Austrian Science Fund FWF P 28135Austrian Science Fund FWF P 30584Austrian Science Fund FWF W 1224Austrian Science Fund FWF W 1261Wellcome Trust
6 · The paper itself

Abstract

MORN (Membrane Occupation and Recognition Nexus) repeat proteins have a wide taxonomic distribution, being found in both prokaryotes and eukaryotes. Despite this ubiquity, they remain poorly characterised at both a structural and a functional level compared to other common repeats. In functional terms, they are often assumed to be lipid-binding modules that mediate membrane targeting. We addressed this putative activity by focusing on a protein composed solely of MORN repeats-Trypanosoma brucei MORN1. Surprisingly, no evidence for binding to membranes or lipid vesicles by TbMORN1 could be obtained either in vivo or in vitro. Conversely, TbMORN1 did interact with individual phospholipids. High- and low-resolution structures of the MORN1 protein from Trypanosoma brucei and homologous proteins from the parasites Toxoplasma gondii and Plasmodium falciparum were obtained using a combination of macromolecular crystallography, small-angle X-ray scattering, and electron microscopy. This enabled a first structure-based definition of the MORN repeat itself. Furthermore, all three structures dimerised via their C-termini in an antiparallel configuration. The dimers could form extended or V-shaped quaternary structures depending on the presence of specific interface residues. This work provides a new perspective on MORN repeats, showing that they are protein-protein interaction modules capable of mediating both dimerisation and oligomerisation.

Indexed as

Repetitive Sequences, Amino AcidAmino Acid SequenceCell MembraneCrystallography, X-RayCytosolLipidsLiposomesPhenotypePhospholipidsProtein BindingProtein MultimerizationProtozoan ProteinsRecombinant ProteinsTrypanosoma brucei bruceiLipidsLiposomesPhospholipidsProtozoan ProteinsRecombinant Proteins

Identifiers

PMID33296386
PMCPMC7725318
OpenAlexW3113068668

What OpenQuestion holds

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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.