Evidence map›Paper›PMID 26605945›Full record

ArticlePloS one2015

SPO73 and SPO71 Function Cooperatively in Prospore Membrane Elongation During Sporulation in Saccharomyces cerevisiae.

Emily M Parodi, Joseph M Roesner, Linda S Huang

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.2field-weighted citation impact, top 43% 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

12 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Roles for the canonical polarity machinery in thebioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Membrane and organelle rearrangement during ascospore formation in budding yeast.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  6. Meiotic Cytokinesis inJournal of fungi (Basel, Switzerland) · 2024
    Review
  7. Cadmium Sulfide Quantum Dots Adversely Affect Gametogenesis inNanomaterials (Basel, Switzerland) · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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

3 authors at 1 institution in 1 country.

Emily M ParodiDepartment of Biology, University of Massachusetts Boston, Boston, Massachusetts, United States of America.
Joseph M RoesnerDepartment of Biology, University of Massachusetts Boston, Boston, Massachusetts, United States of America.
Linda S HuangDepartment of Biology, University of Massachusetts Boston, Boston, Massachusetts, United States of America.
University of Massachusetts Boston · US

Funding

SPO71 function in morphogenesis during spore developmentR15GM086805 · NIGMS · UNIVERSITY OF MASSACHUSETTS BOSTON · PI HUANG, LINDA S. · 2009 to 2025
$2.0M
NIGMS NIH HHS R15 GM086805
6 · The paper itself

Abstract

In the yeast Saccharomyces cerevisiae, cells undergoing sporulation form prospore membranes to surround their meiotic nuclei. The prospore membranes ultimately become the plasma membranes of the new cells. The putative phospholipase Spo1 and the tandem Pleckstrin Homology domain protein Spo71 have previously been shown to be required for prospore membrane development, along with the constitutively expressed Vps13 involved in vacuolar sorting. Here, we utilize genetic analysis, and find that SPO73 is required for proper prospore membrane shape and, like SPO71, is necessary for prospore membrane elongation. Additionally, similar to SPO71, loss of SPO73 partially suppresses spo1Δ. Spo73 localizes to prospore membranes and complexes with Spo71. We also find that phosphatidylserine localizes to the prospore membrane. Our results suggest a model where SPO71 and SPO73 act in opposition to SPO1 to form and elongate prospore membranes, while VPS13 plays a distinct role in prospore membrane development.

Indexed as

Carrier ProteinsCell MembraneGene Knockdown TechniquesLysophospholipaseMultiprotein ComplexesMutationPhenotypePhosphatidylserinesProtein BindingProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpores, FungalCarrier ProteinsLysophospholipaseMultiprotein ComplexesPhosphatidylserinesSaccharomyces cerevisiae ProteinsSPO1 protein, S cerevisiaeSPO71 protein, S cerevisiaeVPS13 protein, S cerevisiae

Identifiers

PMID26605945
PMCPMC4659569
OpenAlexW2184620792

What OpenQuestion holds

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LicenceCC BY
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.