Evidence map›Paper›PMID 22121197›Full record

ArticleThe Journal of biological chemistry2012

Yeast lipin 1 orthologue pah1p regulates vacuole homeostasis and membrane fusion.

Terry Sasser, Quan-Sheng Qiu, Surya Karunakaran, Mark Padolina, Anna Reyes, Blake Flood, Sheena Smith, Chad Gonzales, Rutilio A Fratti

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

69 citing papers in PubMed, 106 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Architecture and function of yeast phosphatidate phosphatase Pah1 domains/regions.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2024
    Review
  10. Article
  11. Article
  12. Article
  13. A Yeast Mitotic Tale for the Nucleus and the Vacuoles to Embrace.International journal of molecular sciences · 2023
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. A review of phosphatidate phosphatase assays.Journal of lipid research · 2020
    Review
  19. Article
  20. Article

9 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

9 authors at 1 institution in 1 country.

Terry SasserDepartment of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
Quan-Sheng Qiu
Surya Karunakaran
Mark Padolina
Anna Reyes
Blake Flood
Sheena Smith
Chad Gonzales
Rutilio A Fratti
University of Illinois Urbana-Champaign · US

Funding

Allosteric Regulation of SNAREs and the Rab GEF Mon1 by PhosphoinositidesR01GM101132 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI FRATTI, RUTILIO A · 2012 to 2016
$1.4M
NIGMS NIH HHS R01 GM101132
6 · The paper itself

Abstract

Vacuole homotypic fusion requires a group of regulatory lipids that includes diacylglycerol, a fusogenic lipid that is produced through multiple metabolic pathways including the dephosphorylation of phosphatidic acid (PA). Here we examined the relationship between membrane fusion and PA phosphatase activity. Pah1p is the single yeast homologue of the Lipin family of PA phosphatases. Deletion of PAH1 was sufficient to cause marked vacuole fragmentation and abolish vacuole fusion. The function of Pah1p solely depended on its phosphatase activity as complementation studies showed that wild type Pah1p restored fusion, whereas the phosphatase dead mutant Pah1p(D398E) had no effect. We discovered that the lack of PA phosphatase activity blocked fusion by inhibiting the binding of SNAREs to Sec18p, an N-ethylmaleimide-sensitive factor homologue responsible for priming inactive cis-SNARE complexes. In addition, pah1Δ vacuoles were devoid of the late endosome/vacuolar Rab Ypt7p, the phosphatidylinositol 3-kinase Vps34p, and Vps39p, a subunit of the HOPS (homotypic fusion and vacuole protein sorting) tethering complex, all of which are required for vacuole fusion. The lack of Vps34p resulted in the absence of phosphatidylinositol 3-phosphate, a lipid required for SNARE activity and vacuole fusion. These findings demonstrate that Pah1p and PA phosphatase activity are critical for vacuole homeostasis and fusion.

Indexed as

Adaptor Proteins, Vesicular TransportAdenosine TriphosphatasesClass III Phosphatidylinositol 3-KinasesHomeostasisIntracellular MembranesMembrane FusionPhosphatidate Phosphataserab GTP-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSNARE ProteinsVacuolesVesicular Transport ProteinsAdaptor Proteins, Vesicular TransportAdenosine TriphosphatasesClass III Phosphatidylinositol 3-KinasesPAH1 protein, S cerevisiaePhosphatidate Phosphataserab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsSEC18 protein, S cerevisiaeSNARE ProteinsVAM6 protein, S cerevisiaeVesicular Transport ProteinsYPT7 protein, S cerevisiae

Identifiers

PMID22121197
PMCPMC3265900
OpenAlexW1986076474

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.