Evidence map›Paper›PMID 32413406›Full record

ArticleJournal of molecular biology2020

Membrane Lipid Requirements of the Lysine Transporter Lyp1 from Saccharomyces cerevisiae.

Joury S van 't Klooster, Tan-Yun Cheng, Hendrik R Sikkema, Aike Jeucken, D Branch Moody, Bert Poolman

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

12 citing papers in PubMed, 19 citations in OpenAlex.

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  3. An in vitro set-up to study Pdr5-mediated substrate translocation.Protein science : a publication of the Protein Society · 2024
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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 3 institutions in 2 countries.

Joury S van 't KloosterDepartment of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747, AG, Groningen, the Netherlands.
Tan-Yun ChengDivision of Rheumatology, Inflammation and Immunity, Brigham and Women's Hospital, Harvard Medical School, 60 Fenwood Road, Boston, MA 02115, USA.
Hendrik R SikkemaDepartment of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747, AG, Groningen, the Netherlands.
Aike JeuckenDepartment of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747, AG, Groningen, the Netherlands.
D Branch MoodyDivision of Rheumatology, Inflammation and Immunity, Brigham and Women's Hospital, Harvard Medical School, 60 Fenwood Road, Boston, MA 02115, USA; Department of Medicine, Harvard Medical School, Boston, MA 02115, USA.
Bert PoolmanDepartment of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747, AG, Groningen, the Netherlands. Electronic address: b.poolman@rug.nl.
University of Groningen · NLBrigham and Women's Hospital · USHarvard University · US

Funding

CD1 Presentation of Self Lipids to Human T CellsR01AR048632 · NIAMS · BRIGHAM AND WOMEN'S HOSPITAL · PI MOODY, DAVID BRANCH · 2002 to 2024
$9.4M
CD1 autoreactive T cells in human inflammatory skin diseaseR37AR048632 · NIAMS · BRIGHAM AND WOMEN'S HOSPITAL · PI DAVID Branch MOODY · 2025 to 2026
$1.1M
NIAMS NIH HHS R01 AR048632NIAMS NIH HHS R37 AR048632
6 · The paper itself

Abstract

Membrane lipids act as solvents and functional cofactors for integral membrane proteins. The yeast plasma membrane is unusual in that it may have a high lipid order, which coincides with low passive permeability for small molecules and a slow lateral diffusion of proteins. Yet, membrane proteins whose functions require altered conformation must have flexibility within membranes. We have determined the molecular composition of yeast plasma membrane lipids located within a defined diameter of model proteins, including the APC-superfamily lysine transporter Lyp1. We now use the composition of lipids that naturally surround Lyp1 to guide testing of lipids that support the normal functioning of the transporter, when reconstituted in vesicles of defined lipid composition. We find that phosphatidylserine and ergosterol are essential for Lyp1 function, and the transport activity displays a sigmoidal relationship with the concentration of these lipids. Non-bilayer lipids stimulate transport activity, but different types are interchangeable. Remarkably, Lyp1 requires a relatively high fraction of lipids with one or more unsaturated acyl chains. The transport data and predictions of the periprotein lipidome of Lyp1 support a new model in which a narrow band of lipids immediately surrounding the transmembrane stalk of a model protein allows conformational changes in the protein.

Indexed as

Amino Acid Transport Systems, BasicCell MembraneKineticsLysineMembrane LipidsMembrane Transport ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAmino Acid Transport Systems, BasicLYP1 protein, S cerevisiaeLysineMembrane LipidsMembrane Transport ProteinsSaccharomyces cerevisiae Proteinsamino acidsAPC superfamilymembrane transportSaccharomyces cerevisiaeyeast plasma membrane

Identifiers

PMID32413406
PMCPMC8005870
OpenAlexW3025125282

What OpenQuestion holds

Textmetadata
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.