Evidence map›Paper›PMID 25954878›Full record

ArticleBiophysical journal2015

MPP1 as a Factor Regulating Phase Separation in Giant Plasma Membrane-Derived Vesicles.

Joanna Podkalicka, Agnieszka Biernatowska, Michał Majkowski, Michał Grzybek, Aleksander F Sikorski

Open access · hybridAbstract read
In one paragraph

Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

17 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Review
  3. EFR3A: a new raft domain organizing protein?Cellular & molecular biology letters · 2023
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  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Peripheral myelin protein 22 preferentially partitions into ordered phase membrane domains.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Flotillins: At the Intersection of ProteinInternational journal of molecular sciences · 2020
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. The Continuing Mystery of Lipid Rafts.Journal of molecular biology · 2016
    Review
  17. 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

5 authors at 2 institutions in 2 countries.

Joanna PodkalickaLaboratory of Cytobiochemistry, Faculty of Biotechnology, University of Wrocław, Wrocław, Poland; Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
Agnieszka BiernatowskaLaboratory of Cytobiochemistry, Faculty of Biotechnology, University of Wrocław, Wrocław, Poland.
Michał MajkowskiLaboratory of Cytobiochemistry, Faculty of Biotechnology, University of Wrocław, Wrocław, Poland.
Michał GrzybekPaul Langerhans Institute Dresden of the Helmholtz Centre Munich at the University Clinic Carl Gustav Carus, TU Dresden, Dresden, Germany; German Center for Diabetes Research (DZD e.v.), Neuherberg, Germany.
Aleksander F SikorskiLaboratory of Cytobiochemistry, Faculty of Biotechnology, University of Wrocław, Wrocław, Poland. Electronic address: afsbc@ibmb.uni.wroc.pl.
University of Wrocław · PLHeinrich Heine University Düsseldorf · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The existence of membrane-rafts helps to conceptually understand the spatiotemporal organization of membrane-associated events (signaling, fusion, fission, etc.). However, as rafts themselves are nanoscopic, dynamic, and transient assemblies, they cannot be directly observed in a metabolizing cell by traditional microscopy. The observation of phase separation in giant plasma membrane-derived vesicles from live cells is a powerful tool for studying lateral heterogeneity in eukaryotic cell membranes, specifically in the context of membrane rafts. Microscopic phase separation is detectable by fluorescent labeling, followed by cooling of the membranes below their miscibility phase transition temperature. It remains unclear, however, if this lipid-driven process is tuneable in any way by interactions with proteins. Here, we demonstrate that MPP1, a member of the MAGUK family, can modulate membrane properties such as the fluidity and phase separation capability of giant plasma membrane-derived vesicles. Our data suggest that physicochemical domain properties of the membrane can be modulated, without major changes in lipid composition, through proteins such as MPP1.

Indexed as

Blood ProteinsCell-Derived MicroparticlesCell Line, TumorCell MembraneHumansMembrane FluidityMembrane ProteinsBlood ProteinsMembrane ProteinsMPP1 protein, human

Identifiers

PMID25954878
PMCPMC4423064
OpenAlexW2145131902

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.