Evidence map›Paper›PMID 35829923›Full record

ArticleCellular and molecular life sciences : CMLS2022

Human myelin proteolipid protein structure and lipid bilayer stacking.

Salla Ruskamo, Arne Raasakka, Jan Skov Pedersen, Anne Martel, Karel Škubník, Tamim Darwish, Lionel Porcar, Petri Kursula

Open access · hybridAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2022. 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
3.9field-weighted citation impact, top 5% 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, 49 citations in OpenAlex.

  1. Review
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  8. Article
  9. Mechanobiology of Myelin Generation/Regeneration in Health and Disease.Results and problems in cell differentiation · 2026
    Review
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  11. Article
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  19. Journal of Zhejiang University. Science. B · 2025
    Review
  20. Review
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

8 authors at 6 institutions in 6 countries.

Salla RuskamoFaculty of Biochemistry and Molecular Medicine & Biocenter Oulu, University of Oulu, Oulu, Finland. salla.ruskamo@oulu.fi.ORCID http://orcid.org/0000-0002-9740-9077
Arne RaasakkaDepartment of Biomedicine, University of Bergen, Bergen, Norway.ORCID http://orcid.org/0000-0002-9443-9959
Jan Skov PedersenDepartment of Chemistry and Interdisciplinary Nanoscience Center (iNANO), Aarhus University, Aarhus, Denmark.
Anne MartelInstitut Laue-Langevin (ILL), Grenoble, France.
Karel ŠkubníkCentral European Institute of Technology, Masaryk University, Brno, Czech Republic.
Tamim DarwishNational Deuteration Facility, The Australian Nuclear Science and Technology Organisation, Locked Bag 2001, Kirrawee DC, Sydney, NSW, 2232, Australia.
Lionel PorcarInstitut Laue-Langevin (ILL), Grenoble, France.
Petri KursulaFaculty of Biochemistry and Molecular Medicine & Biocenter Oulu, University of Oulu, Oulu, Finland. petri.kursula@uib.no.ORCID http://orcid.org/0000-0001-8529-3751
Institut Laue-Langevin · FRUniversity of Bergen · NOAarhus University · DKAustralian Nuclear Science and Technology Organisation · AUCentral European Institute of Technology · CZOulu University of Applied Sciences · FI

Funding

Biotieteiden ja Ympäristön Tutkimuksen Toimikunta 275225
6 · The paper itself

Abstract

The myelin sheath is an essential, multilayered membrane structure that insulates axons, enabling the rapid transmission of nerve impulses. The tetraspan myelin proteolipid protein (PLP) is the most abundant protein of compact myelin in the central nervous system (CNS). The integral membrane protein PLP adheres myelin membranes together and enhances the compaction of myelin, having a fundamental role in myelin stability and axonal support. PLP is linked to severe CNS neuropathies, including inherited Pelizaeus-Merzbacher disease and spastic paraplegia type 2, as well as multiple sclerosis. Nevertheless, the structure, lipid interaction properties, and membrane organization mechanisms of PLP have remained unidentified. We expressed, purified, and structurally characterized human PLP and its shorter isoform DM20. Synchrotron radiation circular dichroism spectroscopy and small-angle X-ray and neutron scattering revealed a dimeric, α-helical conformation for both PLP and DM20 in detergent complexes, and pinpoint structural variations between the isoforms and their influence on protein function. In phosphatidylcholine membranes, reconstituted PLP and DM20 spontaneously induced formation of multilamellar myelin-like membrane assemblies. Cholesterol and sphingomyelin enhanced the membrane organization but were not crucial for membrane stacking. Electron cryomicroscopy, atomic force microscopy, and X-ray diffraction experiments for membrane-embedded PLP/DM20 illustrated effective membrane stacking and ordered organization of membrane assemblies with a repeat distance in line with CNS myelin. Our results shed light on the 3D structure of myelin PLP and DM20, their structure-function differences, as well as fundamental protein-lipid interplay in CNS compact myelin.

Indexed as

Lipid BilayersMyelin Proteolipid ProteinAxonsCentral Nervous SystemHumansMyelin SheathProtein IsoformsLipid BilayersMyelin Proteolipid ProteinProtein IsoformsAtomic force microscopyDM20Integral membrane proteinMyelinProteolipid proteinSmall-angle scattering

Identifiers

PMID35829923
PMCPMC9279222
OpenAlexW4285093617

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.