Evidence map›Paper›PMID 31956022›Full record

ArticleCurrent biology : CB2020

Delineating the Rules for Structural Adaptation of Membrane-Associated Proteins to Evolutionary Changes in Membrane Lipidome.

Maria Makarova, Maria Peter, Gabor Balogh, Attila Glatz, James I MacRae, Nestor Lopez Mora, Paula Booth, Eugene Makeyev, Laszlo Vigh, Snezhana Oliferenko

Open access · hybridAbstract read
In one paragraph

Article in Current biology : CB, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.8field-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

34 citing papers in PubMed, 57 citations in OpenAlex.

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  5. Evolutionary cell biology comes of age.Journal of cell science · 2025
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  6. Formation of giant ER sheets by pentadecanoic acid causes lipotoxicity in fission yeast.Proceedings of the National Academy of Sciences of the United States of America · 2025
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 2 countries.

Maria MakarovaThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK; Randall Centre for Cell and Molecular Biophysics, School of Basic and Medical Biosciences, King's College London, Guy's Campus, London SE1 1UL, UK.
Maria PeterInstitute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Temesvári krt. 62, Szeged 6726, Hungary.
Gabor BaloghInstitute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Temesvári krt. 62, Szeged 6726, Hungary.
Attila GlatzInstitute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Temesvári krt. 62, Szeged 6726, Hungary.
James I MacRaeThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Nestor Lopez MoraDepartment of Chemistry, King's College London, Britannia House, London SE1 1DB, UK.
Paula BoothDepartment of Chemistry, King's College London, Britannia House, London SE1 1DB, UK.
Eugene MakeyevMRC Centre for Developmental Neurobiology, King's College London, Guy's Campus, London SE1 1UL, UK.
Laszlo VighInstitute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Temesvári krt. 62, Szeged 6726, Hungary.
Snezhana OliferenkoThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK; Randall Centre for Cell and Molecular Biophysics, School of Basic and Medical Biosciences, King's College London, Guy's Campus, London SE1 1UL, UK. Electronic address: snezhka.oliferenko@crick.ac.uk.
King's College London · GBHungarian Academy of Sciences · HUHUN-REN Szegedi Biológiai Kutatóközpont · HUThe Francis Crick Institute · GB

Funding

Cancer Research UK FC001002Wellcome Trust 103741/Z/14/ZWellcome Trust 214259Wellcome Trust FC001002
6 · The paper itself

Abstract

Membrane function is fundamental to life. Each species explores membrane lipid diversity within a genetically predefined range of possibilities. How membrane lipid composition in turn defines the functional space available for evolution of membrane-centered processes remains largely unknown. We address this fundamental question using related fission yeasts Schizosaccharomyces pombe and Schizosaccharomyces japonicus. We show that, unlike S. pombe that generates membranes where both glycerophospholipid acyl tails are predominantly 16-18 carbons long, S. japonicus synthesizes unusual "asymmetrical" glycerophospholipids where the tails differ in length by 6-8 carbons. This results in stiffer bilayers with distinct lipid packing properties. Retroengineered S. pombe synthesizing the S.-japonicus-type phospholipids exhibits unfolded protein response and downregulates secretion. Importantly, our protein sequence comparisons and domain swap experiments support the hypothesis that transmembrane helices co-evolve with membranes, suggesting that, on the evolutionary scale, changes in membrane lipid composition may necessitate extensive adaptation of the membrane-associated proteome.

Indexed as

Evolution, MolecularMembrane LipidsMembrane ProteinsNuclear EnvelopeSchizosaccharomycesSpecies SpecificityMembrane LipidsMembrane Proteinsadaptationevolutionfatty acid synthasefission yeastslipid metabolismlipidsmembranestransmembrane proteinsunfolded protein response

Identifiers

PMID31956022
PMCPMC6997885
OpenAlexW2999430643

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.