Evidence map›Paper›PMID 37098755›Full record

ArticleCytoskeleton (Hoboken, N.J.)

Simultaneous co-overexpression of Saccharomyces cerevisiae septins Cdc3 and Cdc10 drives pervasive, phospholipid-, and tag-dependent plasma membrane localization.

Aleyna Benson, Michael McMurray

Open access · greenAbstract read
In one paragraph

Article in Cytoskeleton (Hoboken, N.J.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
  3. Localization and function of septins are susceptible to epitope tagging.bioRxiv : the preprint server for biology · 2025
    Article
  4. Med3-mediated NADPH generation to helpApplied and environmental microbiology · 2024
    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

2 authors at 1 institution in 1 country.

Aleyna BensonDepartment of Cell and Developmental Biology, University of Colorado Anschutz Medical Campus, Aurora, Colorado, USA.
Michael McMurrayDepartment of Cell and Developmental Biology, University of Colorado Anschutz Medical Campus, Aurora, Colorado, USA.ORCID 0000-0002-4615-4334
University of Colorado Anschutz Medical Campus · US

Funding

REGULATION OF HISTIDINE BIOSYNTHESIS IN YEASTR01GM035010 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI FINK, GERALD R · 1985 to 2016
$9.9M
Step-wise order of assembly of histone proteins into nucleosomes in living cellsR35GM148198 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI MICHAEL A MCMURRAY · 2023 to 2026
$1.6M
Requirements for cytosolic chaperones in the de novo folding of septin proteinsR01GM124024 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI MCMURRAY, MICHAEL A · 2017 to 2021
$1.5M
NIGMS NIH HHS R01 GM035010NIGMS NIH HHS R01 GM124024NIGMS NIH HHS R35 GM148198
6 · The paper itself

Abstract

Septin proteins contribute to many eukaryotic processes involving cellular membranes. In the budding yeast Saccharomyces cerevisiae, septin hetero-oligomers interact with the plasma membrane (PM) almost exclusively at the future site of cytokinesis. While multiple mechanisms of membrane recruitment have been identified, including direct interactions with specific phospholipids and curvature-sensitive interactions via amphipathic helices, these do not fully explain why yeast septins do not localize all over the inner leaflet of the PM. While engineering an inducible split-yellow fluorescent protein (YFP) system to measure the kinetics of yeast septin complex assembly, we found that ectopic co-overexpression of two tagged septins, Cdc3 and Cdc10, resulted in nearly uniform PM localization, as well as perturbation of endogenous septin function. Septin localization and function in gametogenesis were also perturbed. PM localization required the C-terminal YFP fragment fused to the C terminus of Cdc3, the septin-associated kinases Cla4 and Gin4, and phosphotidylinositol-4,5-bis-phosphate (PI[4,5]P

Indexed as

Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCell Cycle ProteinsCell MembraneCytokinesisSeptinsCell Cycle ProteinsSaccharomyces cerevisiae ProteinsSeptinsassemblyplasma membraneseptinsyeast

Identifiers

PMID37098755
PMCPMC10524705
OpenAlexW4367048014

What OpenQuestion holds

Textmetadata
LicenceTDM
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.