Cited by 8Lipid Membrane Structure and BehaviorHereditary Neurological DisordersCaveolin-1 and cellular processes

The cytoplasmic tail of myelin protein zero induces morphological changes in lipid membranes

Open access
Krokengen, Oda C., Touma, Christine, Mularski, Anna, Sutinen, Aleksi, Dunkel, Ryan, Ytterdal, Marie, Raasakka, Arne, Mertens, Haydyn D.T. +2 more·2024·Biochimica et Biophysica Acta (BBA) - Biomembranes

Published version of a preprint

Abstract

The major myelin protein expressed by the peripheral nervous system Schwann cells is protein zero (P0), which represents 50% of the total protein content in myelin. This 30-kDa integral membrane protein consists of an immunoglobulin (Ig)-like domain, a transmembrane helix, and a 69-residue C-terminal cytoplasmic tail (P0ct). The basic residues in P0ct contribute to the tight packing of myelin lipid bilayers, and alterations in the tail affect how P0 functions as an adhesion molecule necessary for the stability of compact myelin. Several neurodegenerative neuropathies are related to P0, including the more common Charcot-Marie-Tooth disease (CMT) and Dejerine-Sottas syndrome (DSS) as well as rare cases of motor and sensory polyneuropathy. We found that high P0ct concentrations affected the membrane properties of bicelles and induced a lamellar-to-inverted hexagonal phase transition, which caused bicelles to fuse into long, protein-containing filament-like structures. These structures likely reflect the formation of semicrystalline lipid domains with potential relevance for myelination. Not only is P0ct important for stacking lipid membranes, but time-lapse fluorescence microscopy also shows that it might affect membrane properties during myelination. We further describe recombinant production and low-resolution structural characterization of full-length human P0. Our findings shed light on P0ct effects on membrane properties, and with the successful purification of full-length P0, we have new tools to study the role of P0 in myelin formation and maintenance in vitro.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/j.bbamem.2024.184368

Cites

128 of 128 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

1 of the 129 references couldn’t be matched to a known paper.

Cited by

Sorted by citations

Authors
Krokengen, O. C., Touma, C., Mularski, A., Sutinen, A., Dunkel, R., Ytterdal, M., Raasakka, A., Mertens, H. D. T., Simonsen, A. C., & Kursula, P.
Affiliations
  • University of Bergen (NO)
  • University of Oulu (FI)
  • University of Southern Denmark (DK)
  • Deutsches Elektronen-Synchrotron DESY (DE)
Corresponding author
Kursula, Petri
Venue
Biochimica et Biophysica Acta (BBA) - Biomembranes
Publisher
Elsevier BV
Published
2024-10
Volume
1866
Issue
7
Pages
184368
ISSN
0005-2736 (ISSN-L)
OpenAlex
W4400315566
Cited by
7
References
129
Citations by year
2026: 3 · 2025: 3 · 2024: 1
FWCI
0.95
Type
journal article
Language
en
Open access
Locations
  • Biochimica et Biophysica Acta (BBA) - Biomembranes (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • University of Southern Denmark Research Portal (University of Southern Denmark) (submittedVersion, cc-by)
Funders
  • Diamond Light Source
  • European Commission (EU-H2020, 101004806, HORIZON2020, H2020)
  • VINNOVA (2019‐02496, 2018-07152, 2018-04969)
  • Svenska Forskningsrådet Formas (2018-07152, 2019-02496)
  • Vetenskapsrådet (2018–04969, 07152, 2019–02496, 201807152, 2018-)
  • Universitetet i Bergen
  • Norges Forskningsråd (245922, 245828, 324877)
  • Horizon 2020 Framework Programme (EU‐H2020, 101004806, 2018-07152)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Hereditary Neurological Disorders
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
Keywords
myelin protein zero, Schwann cells, myelin, bicelles, membrane fusion, myelination, Charcot-Marie-Tooth disease, Dejerine-Sottas syndrome, peripheral neuropathy
MeSH terms
Cytoplasm, Humans, Lipid Bilayers, Membrane Lipids, Myelin Sheath, Myelin P0 Protein

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review