Evidence map›Paper›PMID 15889145›Full record

ArticleThe EMBO journal2005

The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth.

Helena Santos-Rosa, Joanne Leung, Neil Grimsey, Sew Peak-Chew, Symeon Siniossoglou

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 232 papers.

0numbers the graph read from it
0cells of the map it votes in
232citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

232 citing papers in PubMed, 403 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The Inner Nuclear Membrane Has a Unique Lipid Signature.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Architecture and function of yeast phosphatidate phosphatase Pah1 domains/regions.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2024
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

172 more citing papers are in PubMed but not listed here.

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 1 country.

Helena Santos-RosaWellcomeTrust/Cancer Research UK Gurdon Institute, Cambridge, UK.
Joanne Leung
Neil Grimsey
Sew Peak-Chew
Symeon Siniossoglou
Wellcome Trust · GBMRC Laboratory of Molecular Biology · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Remodelling of the nuclear membrane is essential for the dynamic changes of nuclear architecture at different stages of the cell cycle and during cell differentiation. The molecular mechanism underlying the regulation of nuclear membrane biogenesis is not known. Here we show that Smp2, the yeast homologue of mammalian lipin, is a key regulator of nuclear membrane growth during the cell cycle. Smp2 is phosphorylated by Cdc28/Cdk1 and dephosphorylated by a nuclear/endoplasmic reticulum (ER) membrane-localized CPD phosphatase complex consisting of Nem1 and Spo7. Loss of either SMP2 or its dephosphorylated form causes transcriptional upregulation of key enzymes involved in lipid biosynthesis concurrent with a massive expansion of the nucleus. Conversely, constitutive dephosphorylation of Smp2 inhibits cell division. We show that Smp2 associates with the promoters of phospholipid biosynthetic enzymes in a Nem1-Spo7-dependent manner. Our data suggest that Smp2 is a critical factor in coordinating phospholipid biosynthesis at the nuclear/ER membrane with nuclear growth during the cell cycle.

Indexed as

CDC28 Protein Kinase, S cerevisiaeCell CycleEndoplasmic ReticulumGene Expression Regulation, FungalLipidsMembrane LipidsMembrane ProteinsMitosisMultienzyme ComplexesNuclear EnvelopeNuclear ProteinsPhosphatidate PhosphatasePhospholipidsPhosphorylationPromoter Regions, GeneticProtein Processing, Post-TranslationalCDC28 Protein Kinase, S cerevisiaeLipidsMembrane LipidsMembrane ProteinsMultienzyme ComplexesNem1 protein, S cerevisiaeNuclear ProteinsPAH1 protein, S cerevisiaePhosphatidate PhosphatasePhospholipidsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSPO7 protein, S cerevisiae

Identifiers

PMID15889145
PMCPMC1142606
OpenAlexW2020725477

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.