Evidence map›Paper›PMID 21490207›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2011

Transport of the major myelin proteolipid protein is directed by VAMP3 and VAMP7.

Anke Feldmann, Jesa Amphornrat, Madeleine Schönherr, Christine Winterstein, Wiebke Möbius, Torben Ruhwedel, Lydia Danglot, Klaus-Armin Nave, Thierry Galli, Dieter Bruns and 2 more

Abstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
–field-weighted citation impact
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

56 citing papers in PubMed.

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  14. Vesicle Fusion in Oligodendrocyte Maturation and Myelination.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
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  18. Cleavage of VAMP2/3 Affects Oligodendrocyte Lineage Development in the Developing Mouse Spinal Cord.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
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  19. Review
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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

12 authors.

Anke FeldmannDepartment of Biology, Molecular Cell Biology, University of Mainz, D-55128 Mainz, Germany.
Jesa Amphornrat
Madeleine Schönherr
Christine Winterstein
Wiebke Möbius
Torben Ruhwedel
Lydia Danglot
Klaus-Armin Nave
Thierry Galli
Dieter Bruns
Jacqueline Trotter
Eva-Maria Krämer-Albers

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CNS myelination by oligodendrocytes requires directed transport of myelin membrane components and a timely and spatially controlled membrane expansion. In this study, we show the functional involvement of the R-soluble N-ethylmaleimide-sensitive factor attachment protein receptor (R-SNARE) proteins VAMP3/cellubrevin and VAMP7/TI-VAMP in myelin membrane trafficking. VAMP3 and VAMP7 colocalize with the major myelin proteolipid protein (PLP) in recycling endosomes and late endosomes/lysosomes, respectively. Interference with VAMP3 or VAMP7 function using small interfering RNA-mediated silencing and exogenous expression of dominant-negative proteins diminished transport of PLP to the oligodendroglial cell surface. In addition, the association of PLP with myelin-like membranes produced by oligodendrocytes cocultured with cortical neurons was reduced. We furthermore identified Syntaxin-4 and Syntaxin-3 as prime acceptor Q-SNAREs of VAMP3 and VAMP7, respectively. Analysis of VAMP3-deficient mice revealed no myelination defects. Interestingly, AP-3δ-deficient mocha mice, which suffer from impaired secretion of lysosome-related organelles and missorting of VAMP7, exhibit a mild dysmyelination characterized by reduced levels of select myelin proteins, including PLP. We conclude that PLP reaches the cell surface via at least two trafficking pathways with distinct regulations: (1) VAMP3 mediates fusion of recycling endosome-derived vesicles with the oligodendroglial plasma membrane in the course of the secretory pathway; (2) VAMP7 controls exocytosis of PLP from late endosomal/lysosomal organelles as part of a transcytosis pathway. Our in vivo data suggest that exocytosis of lysosome-related organelles controlled by VAMP7 contributes to myelin biogenesis by delivering cargo to the myelin membrane.

Indexed as

AnimalsBiological Transport, ActiveCell MembraneCells, CulturedElectrophoresis, Polyacrylamide GelEndosomesEnzyme-Linked Immunosorbent AssayExocytosisFemaleGenetic VectorsImage Processing, Computer-AssistedImmunohistochemistryLysosomesMaleMiceMice, Inbred C57BLMyelin Proteolipid ProteinR-SNARE ProteinsSybl1 protein, mouseVesicle-Associated Membrane Protein 3

Identifiers

PMID21490207
PMCPMC6622839

What OpenQuestion holds

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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.