Evidence map›Paper›PMID 26432634›Full record

ArticleEukaryotic cell2015

Yeast Integral Membrane Proteins Apq12, Brl1, and Brr6 Form a Complex Important for Regulation of Membrane Homeostasis and Nuclear Pore Complex Biogenesis.

Museer A Lone, Aaron E Atkinson, Christine A Hodge, Stéphanie Cottier, Fernando Martínez-Montañés, Shelley Maithel, Laurent Mène-Saffrané, Charles N Cole, Roger Schneiter

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

28 citing papers in PubMed, 43 citations in OpenAlex.

  1. Atg39-dependent nucleophagy and Atg40-dependent ER-phagy require the Apq12/Brr6/Brl1 complex.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  14. The LEM-ESCRT toolkit: Repair and maintenance of the nucleus.Frontiers in cell and developmental biology · 2022
    Review
  15. Article
  16. Article
  17. A mutation in budding yeastmicroPublication biology · 2021
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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

9 authors at 2 institutions in 2 countries.

Museer A LoneDepartment of Biology, University of Fribourg, Fribourg, Switzerland.
Aaron E AtkinsonGeisel School of Medicine at Dartmouth, Hanover, New Hampshire, USA.
Christine A HodgeGeisel School of Medicine at Dartmouth, Hanover, New Hampshire, USA.
Stéphanie CottierDepartment of Biology, University of Fribourg, Fribourg, Switzerland.
Fernando Martínez-MontañésDepartment of Biology, University of Fribourg, Fribourg, Switzerland.
Shelley MaithelGeisel School of Medicine at Dartmouth, Hanover, New Hampshire, USA.
Laurent Mène-SaffranéDepartment of Biology, University of Fribourg, Fribourg, Switzerland.
Charles N ColeGeisel School of Medicine at Dartmouth, Hanover, New Hampshire, USA charles.cole@dartmouth.edu roger.schneiter@unifr.ch.
Roger SchneiterDepartment of Biology, University of Fribourg, Fribourg, Switzerland charles.cole@dartmouth.edu roger.schneiter@unifr.ch.
University of Fribourg · CHDartmouth College · US

Funding

Translational Engineering in Cancer (TEC)P30CA023108 · NCI · DARTMOUTH COLLEGE · PI Steven D Leach · 1985 to 2026
$91.3M
NCI NIH HHS P30 CA023108
6 · The paper itself

Abstract

Proper functioning of intracellular membranes is critical for many cellular processes. A key feature of membranes is their ability to adapt to changes in environmental conditions by adjusting their composition so as to maintain constant biophysical properties, including fluidity and flexibility. Similar changes in the biophysical properties of membranes likely occur when intracellular processes, such as vesicle formation and fusion, require dramatic changes in membrane curvature. Similar modifications must also be made when nuclear pore complexes (NPCs) are constructed within the existing nuclear membrane, as occurs during interphase in all eukaryotes. Here we report on the role of the essential nuclear envelope/endoplasmic reticulum (NE/ER) protein Brl1 in regulating the membrane composition of the NE/ER. We show that Brl1 and two other proteins characterized previously-Brr6, which is closely related to Brl1, and Apq12-function together and are required for lipid homeostasis. All three transmembrane proteins are localized to the NE and can be coprecipitated. As has been shown for mutations affecting Brr6 and Apq12, mutations in Brl1 lead to defects in lipid metabolism, increased sensitivity to drugs that inhibit enzymes involved in lipid synthesis, and strong genetic interactions with mutations affecting lipid metabolism. Mutations affecting Brl1 or Brr6 or the absence of Apq12 leads to hyperfluid membranes, because mutant cells are hypersensitive to agents that increase membrane fluidity. We suggest that the defects in nuclear pore complex biogenesis and mRNA export seen in these mutants are consequences of defects in maintaining the biophysical properties of the NE.

Indexed as

Organelle BiogenesisAdaptation, PhysiologicalBenzyl AlcoholEpistasis, GeneticHomeostasisMembrane LipidsMembrane ProteinsMutationNuclear EnvelopeNuclear Pore Complex ProteinsRNA, MessengerRNA TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSterolsViscosityBenzyl AlcoholMembrane LipidsMembrane ProteinsNuclear Pore Complex ProteinsRNA, MessengerSaccharomyces cerevisiae ProteinsSterols

Identifiers

PMID26432634
PMCPMC4664871
OpenAlexW2181918089

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.