Evidence map›Paper›PMID 20016074›Full record

ArticleJournal of cell science2010

Integral membrane proteins Brr6 and Apq12 link assembly of the nuclear pore complex to lipid homeostasis in the endoplasmic reticulum.

Christine A Hodge, Vineet Choudhary, Michael J Wolyniak, John J Scarcelli, Roger Schneiter, Charles N Cole

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing 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

48 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. The role of lipids in genome integrity and pluripotency.Biochemical Society transactions · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. The Many Faces of Lipids in Genome Stability (and How to Unmask Them).International journal of molecular sciences · 2021
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. A mutation in budding yeastmicroPublication biology · 2021
    Article
  17. Article
  18. Article
  19. Article
  20. Review
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 2 institutions in 2 countries.

Christine A HodgeDepartment of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA.
Vineet Choudhary
Michael J Wolyniak
John J Scarcelli
Roger Schneiter
Charles N Cole
Dartmouth College · USUniversity of Fribourg · CH

Funding

REGULATION OF THE METABOLISM OF EUCARYOTIC MRNAR01GM033998 · NIGMS · DARTMOUTH COLLEGE · PI COLE, CHARLES N. · 1985 to 2013
$6.1M
Howard Hughes Medical InstituteNIGMS NIH HHS GM33998NIGMS NIH HHS R01 GM033998
6 · The paper itself

Abstract

Cells of Saccharomyces cerevisiae lacking Apq12, a nuclear envelope (NE)-endoplasmic reticulum (ER) integral membrane protein, are defective in assembly of nuclear pore complexes (NPCs), possibly because of defects in regulating membrane fluidity. We identified BRR6, which encodes an essential integral membrane protein of the NE-ER, as a dosage suppressor of apq12 Delta. Cells carrying the temperature-sensitive brr6-1 allele have been shown to have defects in nucleoporin localization, mRNA metabolism and nuclear transport. Electron microscopy revealed that brr6-1 cells have gross NE abnormalities and proliferation of the ER. brr6-1 cells were hypersensitive to compounds that affect membrane biophysical properties and to inhibitors of lipid biosynthetic pathways, and displayed strong genetic interactions with genes encoding non-essential lipid biosynthetic enzymes. Strikingly, brr6-1 cells accumulated, in or near the NE, elevated levels of the two classes of neutral lipids, steryl esters and triacylglycerols, and over-accumulated sterols when they were provided exogenously. Although neutral lipid synthesis is dispensable in wild-type cells, viability of brr6-1 cells was fully dependent on neutral lipid production. These data indicate that Brr6 has an essential function in regulating lipid homeostasis in the NE-ER, thereby impacting NPC formation and nucleocytoplasmic transport.

Indexed as

Active Transport, Cell NucleusCell NucleusEndoplasmic ReticulumLipid MetabolismMembrane FluidityMembrane ProteinsMutant ProteinsNuclear EnvelopeNuclear PoreNuclear ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSterolsTemperatureTriglyceridesApq12 protein, S cerevisiaeBrr6 protein, S cerevisiaeMembrane ProteinsMutant ProteinsNuclear ProteinsSaccharomyces cerevisiae ProteinsSterolsTriglycerides

Identifiers

PMID20016074
PMCPMC2794714
OpenAlexW2146156912

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.