Evidence map›Paper›PMID 29066609›Full record

ArticleThe Journal of cell biology2017

Membrane curvature directs the localization of Cdc42p to novel foci required for cell-cell fusion.

Jean A Smith, Allison E Hall, Mark D Rose

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2017. 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
0.9field-weighted citation impact, top 26% 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, 24 citations in OpenAlex.

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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

3 authors at 2 institutions in 1 country.

Jean A SmithDepartment of Molecular Biology, Princeton University, Princeton, NJ.
Allison E HallDepartment of Molecular Biology, Princeton University, Princeton, NJ.
Mark D RoseDepartment of Molecular Biology, Princeton University, Princeton, NJ mark.rose@georgetown.edu.ORCID 0000-0003-1112-4765
Princeton University · USGeorgetown University · US

Funding

PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM007388 · NIGMS · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 1985 to 2022
$27.4M
Mechanisms of Nuclear and Cell Fusion in YeastR01GM037739 · NIGMS · PRINCETON UNIVERSITY · PI ROSE, MARK DAVID · 1987 to 2016
$7.4M
NIGMS NIH HHS R01 GM037739NIGMS NIH HHS T32 GM007388
6 · The paper itself

Abstract

Cell fusion is ubiquitous in eukaryotic fertilization and development. The highly conserved Rho-GTPase Cdc42p promotes yeast fusion through interaction with Fus2p, a pheromone-induced amphiphysin-like protein. We show that in prezygotes, Cdc42p forms a novel Fus2p-dependent focus at the center of the zone of cell fusion (ZCF) and remains associated with remnant cell walls after initial fusion. At the ZCF and during fusion, Cdc42p and Fus2p colocalized. In contrast, in shmoos, both proteins were near the cortex but spatially separate. Cdc42p focus formation depends on ZCF membrane curvature: mutant analysis showed that Cdc42p localization is negatively affected by shmoo-like positive ZCF curvature, consistent with the flattening of the ZCF during fusion. BAR-domain proteins such as the fusion proteins Fus2p and Rvs161p are known to recognize membrane curvature. We find that mutations that disrupt binding of the Fus2p/Rvs161p heterodimer to membranes affect Cdc42p ZCF localization. We propose that Fus2p localizes Cdc42p to the flat ZCF to promote cell wall degradation.

Indexed as

Gene Expression Regulation, Fungalcdc42 GTP-Binding Protein, Saccharomyces cerevisiaeCell FusionCell MembraneCell WallCytoskeletal ProteinsGenes, ReporterGreen Fluorescent ProteinsHydrolysisLuminescent ProteinsMating FactorMembrane ProteinsMutationPhosphorylationProtein BindingProtein Multimerizationcdc42 GTP-Binding Protein, Saccharomyces cerevisiaeCytoskeletal ProteinsFUS2 protein, S cerevisiaeGreen Fluorescent ProteinsLuminescent ProteinsMating FactorMembrane ProteinsRed Fluorescent ProteinRVS161 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID29066609
PMCPMC5716282
OpenAlexW2766717912

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.