Evidence map›Paper›PMID 30550553›Full record

ArticlePloS one2018

Glucosylceramide acyl chain length is sensed by the glycolipid transfer protein.

Anders P E Backman, Josefin Halin, Henrik Nurmi, Anna Möuts, Matti A Kjellberg, Peter Mattjus

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

13 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
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  10. Pathological α-syn aggregation is mediated by glycosphingolipid chain length and the physiological state of α-syn in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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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

6 authors at 1 institution in 1 country.

Anders P E BackmanBiochemistry, Faculty of Science and Engineering Åbo Akademi University, Artillerigatan 6A, III, FI Turku, Finland.
Josefin HalinBiochemistry, Faculty of Science and Engineering Åbo Akademi University, Artillerigatan 6A, III, FI Turku, Finland.
Henrik NurmiBiochemistry, Faculty of Science and Engineering Åbo Akademi University, Artillerigatan 6A, III, FI Turku, Finland.
Anna MöutsBiochemistry, Faculty of Science and Engineering Åbo Akademi University, Artillerigatan 6A, III, FI Turku, Finland.
Matti A KjellbergBiochemistry, Faculty of Science and Engineering Åbo Akademi University, Artillerigatan 6A, III, FI Turku, Finland.
Peter MattjusBiochemistry, Faculty of Science and Engineering Åbo Akademi University, Artillerigatan 6A, III, FI Turku, Finland.ORCID 0000-0001-8991-5933
Åbo Akademi University · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The glycolipid transfer protein, GLTP, can be found in the cytoplasm, and it has a FFAT-like motif (two phenylalanines in an acidic tract) that targets it to the endoplasmic reticulum (ER). We have previously shown that GLTP can bind to a transmembrane ER protein, vesicle-associated membrane protein-associated protein A (VAP-A), which is involved in a wide range of ER functions. We have addressed the mechanisms that might regulate the association between GLTP and the VAP proteins by studying the capacity of GLTP to recognize different N-linked acyl chain species of glucosylceramide. We used surface plasmon resonance and a lipid transfer competition assay to show that GLTP prefers shorter N-linked fully saturated acyl chain glucosylceramides, such as C8, C12, and C16, whereas long C18, C20, and C24-glucosylceramides are all bound more weakly and transported more slowly than their shorter counterparts. Changes in the intrinsic GLTP tryptophan fluorescence blueshifts, also indicate a break-point between C16- and C18-glucosylceramide in the GLTP sensing ability. It has long been postulated that GLTP would be a sensor in the sphingolipid synthesis machinery, but how this mechanistically occurs has not been addressed before. It is unclear what proteins the GLTP VAP association would influence. Here we found that if GLTP has a bound GlcCer the association with VAP-A is weaker. We have also used a formula for identifying putative FFAT-domains, and we identified several potential VAP-interactors within the ceramide and sphingolipid synthesis pathways that could be candidates for regulation by GLTP.

Indexed as

AnimalsCarrier ProteinsCattleEscherichia coliGlucosylceramidesMembranes, ArtificialMolecular StructurePhosphatidylcholinesProtein ConformationSurface Plasmon ResonanceTryptophan1-palmitoyl-2-oleoylphosphatidylcholineCarrier ProteinsGlucosylceramideslipid transfer proteinMembranes, ArtificialPhosphatidylcholinesTryptophan

Identifiers

PMID30550553
PMCPMC6294359
OpenAlexW2905039340

What OpenQuestion holds

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LicenceCC BY
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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.