Evidence map›Paper›PMID 21849510›Full record

ArticleThe Journal of biological chemistry2011

Topology of 1-acyl-sn-glycerol-3-phosphate acyltransferases SLC1 and ALE1 and related membrane-bound O-acyltransferases (MBOATs) of Saccharomyces cerevisiae.

Martin Pagac, Hector Vazquez de la Mora, Cécile Duperrex, Carole Roubaty, Christine Vionnet, Andreas Conzelmann

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. 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
3.3field-weighted citation impact, top 8% 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, 59 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Phosphatidic acid biosynthesis in the model organism yeast Saccharomyces cerevisiae - a survey.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2021
    Review
  6. Article
  7. An overview of ghrelinExpert opinion on therapeutic patents · 2020
    Review
  8. Article
  9. Phospholipid turnover and acyl chain remodeling in the yeast ER.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Mitochondrial phospholipids: role in mitochondrial function.Journal of bioenergetics and biomembranes · 2016
    Review
  15. Article
  16. Article
  17. Article
  18. Lipid droplet dynamics in budding yeast.Cellular and molecular life sciences : CMLS · 2015
    Review
  19. Article
  20. 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 at 1 institution in 1 country.

Martin PagacDepartment of Biology, University of Fribourg, CH-1700 Fribourg, Switzerland.
Hector Vazquez de la Mora
Cécile Duperrex
Carole Roubaty
Christine Vionnet
Andreas Conzelmann
University of Fribourg · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In yeast, phosphatidic acid, the biosynthetic precursor for all glycerophospholipids and triacylglycerols, is made de novo by the 1-acyl-sn-glycerol-3-phosphate acyltransferases Ale1p and Slc1p. Ale1p belongs to the membrane-bound O-acyltransferase (MBOAT) family, which contains many enzymes acylating lipids but also others that acylate secretory proteins residing in the lumen of the ER. A histidine present in a very short loop between two predicted transmembrane domains is the only residue that is conserved throughout the MBOAT gene family. The yeast MBOAT proteins of known function comprise Ale1p, the ergosterol acyltransferases Are1p and Are2p, and Gup1p, the last of which acylates lysophosphatidylinositol moieties of GPI anchors on ER lumenal GPI proteins. C-terminal topology reporters added to truncated versions of Gup1p yield a topology predicting a lumenal location of its uniquely conserved histidine 447 residue. The same approach shows that Ale1p and Are2p also have the uniquely conserved histidine residing in the ER lumen. Because these data raised the possibility that phosphatidic acid could be made in the lumen of the ER, we further investigated the topology of the second yeast 1-acyl-sn-glycerol-3-phosphate acyltransferase, Slc1p. The location of C-terminal topology reporters, microsomal assays probing the protease sensitivity of inserted tags, and the accessibility of natural or artificially inserted cysteines to membrane-impermeant alkylating agents all indicate that the most conserved motif containing the presumed active site histidine of Slc1p is oriented toward the ER lumen, whereas other conserved motifs are cytosolic. The implications of these findings are discussed.

Indexed as

AcyltransferasesDyneinsEndoplasmic ReticulumIntracellular MembranesMembrane Transport ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSterol O-AcyltransferaseAcyltransferasesARE2 protein, S cerevisiaeDyneinsGup1 protein, S cerevisiaeMembrane Transport ProteinsSaccharomyces cerevisiae ProteinsSLC1 protein, S cerevisiaeSterol O-Acyltransferase

Identifiers

PMID21849510
PMCPMC3196135
OpenAlexW2045796707

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.