Evidence map›Paper›PMID 23344949›Full record

ArticleThe Journal of biological chemistry2013

Alteration of plasma membrane organization by an anticancer lysophosphatidylcholine analogue induces intracellular acidification and internalization of plasma membrane transporters in yeast.

Ola Czyz, Teshager Bitew, Alvaro Cuesta-Marbán, Christopher R McMaster, Faustino Mollinedo, Vanina Zaremberg

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

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  15. Article
  16. Lipids and cell death in yeast.FEMS yeast research · 2014
    Review
  17. Article
  18. 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

6 authors.

Ola CzyzDepartment of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada.
Teshager BitewDepartment of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada.
Alvaro Cuesta-MarbánInstituto de Biología Molecular y Celular del Cáncer, Centro de Investigación del Cáncer, Consejo Superior de Investigaciones Científicas-Universidad de Salamanca, Campus Miguel de Unamuno, E-37007 Salamanca, Spain.
Christopher R McMasterDepartment of Pharmacology, Atlantic Research Centre, Dalhousie University, Halifax, Nova Scotia B3H 4H7, Canada.
Faustino MollinedoInstituto de Biología Molecular y Celular del Cáncer, Centro de Investigación del Cáncer, Consejo Superior de Investigaciones Científicas-Universidad de Salamanca, Campus Miguel de Unamuno, E-37007 Salamanca, Spain. Electronic address: fmollin@usal.es.
Vanina ZarembergDepartment of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada. Electronic address: vzarembe@ucalgary.ca.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The lysophosphatidylcholine analogue edelfosine is a potent antitumor lipid that targets cellular membranes. The underlying mechanisms leading to cell death remain controversial, although two cellular membranes have emerged as primary targets of edelfosine, the plasma membrane (PM) and the endoplasmic reticulum. In an effort to identify conditions that enhance or prevent the cytotoxic effect of edelfosine, we have conducted genome-wide surveys of edelfosine sensitivity and resistance in Saccharomyces cerevisiae presented in this work and the accompanying paper (Cuesta-Marbán, Á., Botet, J., Czyz, O., Cacharro, L. M., Gajate, C., Hornillos, V., Delgado, J., Zhang, H., Amat-Guerri, F., Acuña, A. U., McMaster, C. R., Revuelta, J. L., Zaremberg, V., and Mollinedo, F. (January 23, 2013) J. Biol. Chem. 288,), respectively. Our results point to maintenance of pH homeostasis as a major player in modulating susceptibility to edelfosine with the PM proton pump Pma1p playing a main role. We demonstrate that edelfosine alters PM organization and induces intracellular acidification. Significantly, we show that edelfosine selectively reduces lateral segregation of PM proteins like Pma1p and nutrient H(+)-symporters inducing their ubiquitination and internalization. The biology associated to the mode of action of edelfosine we have unveiled includes selective modification of lipid raft integrity altering pH homeostasis, which in turn regulates cell growth.

Indexed as

Amino Acid Transport Systems, BasicAntineoplastic AgentsCell MembraneDrug Screening Assays, AntitumorHydrogen-Ion ConcentrationIntracellular FluidIntracellular MembranesMembrane MicrodomainsMicrobial ViabilityNucleotide Transport ProteinsPhospholipid EthersProtein TransportProton-Translocating ATPasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence DeletionAmino Acid Transport Systems, BasicAntineoplastic AgentsCAN1 protein, S cerevisiaeedelfosineFUR4 protein, S cerevisiaeNucleotide Transport ProteinsPhospholipid EthersPMA1 protein, S cerevisiaeProton-Translocating ATPasesSaccharomyces cerevisiae Proteins

Identifiers

PMID23344949
PMCPMC3605658

What OpenQuestion holds

Textmetadata
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.