Evidence map›Paper›PMID 24390141›Full record

ArticleEukaryotic cell2014

A visual screen of protein localization during sporulation identifies new components of prospore membrane-associated complexes in budding yeast.

Chien Lam, Ethan Santore, Elizabeth Lavoie, Leor Needleman, Nicholas Fiacco, Carey Kim, Aaron M Neiman

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

22 citing papers in PubMed, 30 citations in OpenAlex.

  1. The Predicted Structure ofJournal of fungi (Basel, Switzerland) · 2025
    Article
  2. Review
  3. Membrane and organelle rearrangement during ascospore formation in budding yeast.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  4. Article
  5. Meiotic Cytokinesis inJournal of fungi (Basel, Switzerland) · 2024
    Review
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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

7 authors at 1 institution in 1 country.

Chien LamDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York, USA.
Ethan Santore
Elizabeth Lavoie
Leor Needleman
Nicholas Fiacco
Carey Kim
Aaron M Neiman
Stony Brook University · US

Funding

Equipment supplement for grant R01 GM072540 Assembly and Function of the Yeast Spore Wall.R01GM072540 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI NEIMAN, AARON M · 2005 to 2025
$7.1M
NIGMS NIH HHS GM072540NIGMS NIH HHS R01 GM072540
6 · The paper itself

Abstract

During ascospore formation in Saccharomyces cerevisiae, the secretory pathway is reorganized to create new intracellular compartments, termed prospore membranes. Prospore membranes engulf the nuclei produced by the meiotic divisions, giving rise to individual spores. The shape and growth of prospore membranes are constrained by cytoskeletal structures, such as septin proteins, that associate with the membranes. Green fluorescent protein (GFP) fusions to various proteins that associate with septins at the bud neck during vegetative growth as well as to proteins encoded by genes that are transcriptionally induced during sporulation were examined for their cellular localization during prospore membrane growth. We report localizations for over 100 different GFP fusions, including over 30 proteins localized to the prospore membrane compartment. In particular, the screen identified IRC10 as a new component of the leading-edge protein complex (LEP), a ring structure localized to the lip of the prospore membrane. Localization of Irc10 to the leading edge is dependent on SSP1, but not ADY3. Loss of IRC10 caused no obvious phenotype, but an ady3 irc10 mutant was completely defective in sporulation and displayed prospore membrane morphologies similar to those of an ssp1 strain. These results reveal the architecture of the LEP and provide insight into the evolution of this membrane-organizing complex.

Indexed as

Amino Acid SequenceCell Cycle ProteinsCell MembraneMembrane ProteinsMolecular Sequence DataPhenotypeProtein BindingProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpores, FungalADY3 protein, S cerevisiaeCell Cycle ProteinsIRC10 protein, S cerevisiaeMembrane ProteinsSaccharomyces cerevisiae ProteinsSSP1 protein, S cerevisiae

Identifiers

PMID24390141
PMCPMC3957589
OpenAlexW2149001850

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.