Evidence map›Paper›PMID 25368380›Full record

ArticleMolecular and cellular biology2015

The major myelin-resident protein PLP is transported to myelin membranes via a transcytotic mechanism: involvement of sulfatide.

Wia Baron, Hande Ozgen, Bert Klunder, Jenny C de Jonge, Anita Nomden, Annechien Plat, Elisabeth Trifilieff, Hans de Vries, Dick Hoekstra

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

20 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Microcephaly in Neurometabolic Diseases.Children (Basel, Switzerland) · 2022
    Review
  9. Review
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Oligodendroglial membrane dynamics in relation to myelin biogenesis.Cellular and molecular life sciences : CMLS · 2016
    Review
  17. Review
  18. Article
  19. Article
  20. 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

9 authors at 3 institutions in 2 countries.

Wia BaronDepartment of Cell Biology, University of Groningen, University Medical Center Groningen, Groningen, The Netherlands w.baron@umcg.nl.
Hande OzgenDepartment of Cell Biology, University of Groningen, University Medical Center Groningen, Groningen, The Netherlands.
Bert KlunderDepartment of Cell Biology, University of Groningen, University Medical Center Groningen, Groningen, The Netherlands.
Jenny C de JongeDepartment of Cell Biology, University of Groningen, University Medical Center Groningen, Groningen, The Netherlands.
Anita NomdenDepartment of Cell Biology, University of Groningen, University Medical Center Groningen, Groningen, The Netherlands.
Annechien PlatDepartment of Cell Biology, University of Groningen, University Medical Center Groningen, Groningen, The Netherlands.
Elisabeth TrifilieffUMR_S U1119 INSERM/Université de Strasbourg, Faculté de Médecine, Strasbourg, France.
Hans de VriesDepartment of Cell Biology, University of Groningen, University Medical Center Groningen, Groningen, The Netherlands.
Dick HoekstraDepartment of Cell Biology, University of Groningen, University Medical Center Groningen, Groningen, The Netherlands.
University Medical Center Groningen · NLUniversity of Groningen · NLUniversité de Strasbourg · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Myelin membranes are sheet-like extensions of oligodendrocytes that can be considered membrane domains distinct from the cell's plasma membrane. Consistent with the polarized nature of oligodendrocytes, we demonstrate that transcytotic transport of the major myelin-resident protein proteolipid protein (PLP) is a key element in the mechanism of myelin assembly. Upon biosynthesis, PLP traffics to myelin membranes via syntaxin 3-mediated docking at the apical-surface-like cell body plasma membrane, which is followed by subsequent internalization and transport to the basolateral-surface-like myelin sheet. Pulse-chase experiments, in conjunction with surface biotinylation and organelle fractionation, reveal that following biosynthesis, PLP is transported to the cell body surface in Triton X-100 (TX-100)-resistant microdomains. At the plasma membrane, PLP transiently resides within these microdomains and its lateral dissipation is followed by segregation into 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate (CHAPS)-resistant domains, internalization, and subsequent transport toward the myelin membrane. Sulfatide triggers PLP's reallocation from TX-100- into CHAPS-resistant membrane domains, while inhibition of sulfatide biosynthesis inhibits transcytotic PLP transport. Taking these findings together, we propose a model in which PLP transport to the myelin membrane proceeds via a transcytotic mechanism mediated by sulfatide and characterized by a conformational alteration and dynamic, i.e., transient, partitioning of PLP into distinct membrane microdomains involved in biosynthetic and transcytotic transport.

Indexed as

AnimalsBiological TransportBiotinylationCell MembraneDetergentsEpitopesHep G2 CellsHumansMembrane MicrodomainsMyelin Proteolipid ProteinMyelin SheathOctoxynolProtein Structure, TertiaryRatsRats, WistarSulfoglycosphingolipidsDetergentsEpitopesMyelin Proteolipid ProteinOctoxynolSulfoglycosphingolipids

Identifiers

PMID25368380
PMCPMC4295386
OpenAlexW2048177784

What OpenQuestion holds

Textmetadata
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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.