Evidence map›Paper›PMID 29976762›Full record

ArticleThe EMBO journal2018

Lateral plasma membrane compartmentalization links protein function and turnover.

Jon V Busto, Annegret Elting, Daniel Haase, Felix Spira, Julian Kuhlman, Marco Schäfer-Herte, Roland Wedlich-Söldner

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

29 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Inducible degradation-coupled phosphoproteomics identifies PP2AFrontiers in cell and developmental biology · 2024
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  8. High Electrochemiluminescence from Ru(bpy)Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Article
  9. Article
  10. α-Arrestins and Their Functions: From Yeast to Human Health.International journal of molecular sciences · 2022
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Plasma Membrane MCC/Eisosome Domains Promote Stress Resistance in Fungi.Microbiology and molecular biology reviews : MMBR · 2020
    Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Jon V BustoInstitute of Cell Dynamics and Imaging, Cells-In-Motion Cluster of Excellence (EXC1003 - CiM), University of Münster, Münster, Germany.
Annegret EltingInstitute of Cell Dynamics and Imaging, Cells-In-Motion Cluster of Excellence (EXC1003 - CiM), University of Münster, Münster, Germany.
Daniel HaaseInstitute of Cell Dynamics and Imaging, Cells-In-Motion Cluster of Excellence (EXC1003 - CiM), University of Münster, Münster, Germany.
Felix SpiraInstitute of Cell Dynamics and Imaging, Cells-In-Motion Cluster of Excellence (EXC1003 - CiM), University of Münster, Münster, Germany.
Julian KuhlmanInstitute of Cell Dynamics and Imaging, Cells-In-Motion Cluster of Excellence (EXC1003 - CiM), University of Münster, Münster, Germany.
Marco Schäfer-HerteInstitute of Cell Dynamics and Imaging, Cells-In-Motion Cluster of Excellence (EXC1003 - CiM), University of Münster, Münster, Germany.
Roland Wedlich-SöldnerInstitute of Cell Dynamics and Imaging, Cells-In-Motion Cluster of Excellence (EXC1003 - CiM), University of Münster, Münster, Germany wedlich@uni-muenster.de.ORCID 0000-0002-1364-7589
University of Münster · DEUniversity of the Basque Country · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biological membranes organize their proteins and lipids into nano- and microscale patterns. In the yeast plasma membrane (PM), constituents segregate into a large number of distinct domains. However, whether and how this intricate patchwork contributes to biological functions at the PM is still poorly understood. Here, we reveal an elaborate interplay between PM compartmentalization, physiological function, and endocytic turnover. Using the methionine permease Mup1 as model system, we demonstrate that this transporter segregates into PM clusters. Clustering requires sphingolipids, the tetraspanner protein Nce102, and signaling through TORC2. Importantly, we show that during substrate transport, a simple conformational change in Mup1 mediates rapid relocation into a unique disperse network at the PM Clustered Mup1 is protected from turnover, whereas relocated Mup1 actively recruits the endocytic machinery thereby initiating its own turnover. Our findings suggest that lateral compartmentalization provides an important regulatory link between function and turnover of PM proteins.

Indexed as

Cell MembraneMechanistic Target of Rapamycin Complex 2ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinsmajor urinary proteinsMechanistic Target of Rapamycin Complex 2NCE102 protein, S cerevisiaeProteinsSaccharomyces cerevisiae Proteinsamino acid permeaseendocytosislateral membrane segregationpatchwork membraneplasma membrane

Identifiers

PMID29976762
PMCPMC6092676
OpenAlexW2789671635

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.