Evidence map›Paper›PMID 19531587›Full record

ArticleJournal of cell science2009

The yeast endocytic protein Epsin 2 functions in a cell-division signaling pathway.

Debarati Mukherjee, Brian G Coon, Daniel F Edwards, Claudia B Hanna, Silvia A Longhi, J Michael McCaffery, Beverly Wendland, Lilia A Retegui, Erfei Bi, R Claudio Aguilar

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  4. Endocytic proteins with prion-like domains form viscoelastic condensates that enable membrane remodeling.Proceedings of the National Academy of Sciences of the United States of America · 2021
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

10 authors at 4 institutions in 2 countries.

Debarati MukherjeeDepartment of Biological Sciences, Purdue Cancer Center, Purdue University, West Lafayette, IN 47907, USA.
Brian G Coon
Daniel F Edwards
Claudia B Hanna
Silvia A Longhi
J Michael McCaffery
Beverly Wendland
Lilia A Retegui
Erfei Bi
R Claudio Aguilar
Purdue University West Lafayette · USJohns Hopkins University · USUniversity of Buenos Aires · ARUniversity of Pennsylvania · US

Funding

SIGNALING MECHANISMS IN CELL POLARITY IN YEASTR01GM059216 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI BI, ERFEI · 1999 to 2012
$3.8M
NIGMS NIH HHS GM59216
6 · The paper itself

Abstract

The epsins are a family of adaptors involved in recruiting other endocytic proteins, binding of ubiquitylated cargo and induction of membrane curvature. These molecules bear a characteristic epsin N-terminal homology (ENTH) domain and multiple peptide motifs that mediate protein-protein interactions. We have previously demonstrated that the ENTH domain of epsin is involved in Cdc42 signaling regulation. Here, we present evidence that yeast epsin 2 (Ent2) plays a signaling role during cell division. We observed that overexpression of the ENTH domain of Ent2 (ENTH2), but not Ent1, promoted the formation of chains of cells and aberrant septa. This dominant-negative effect resulted from ENTH2-mediated interference with septin assembly pathways. We mapped the ENTH2 determinants responsible for induction of the phenotype and found them to be important for efficient binding to the septin regulatory protein, Bem3. Supporting a physiological role for epsin 2 in cell division, the protein localized to sites of polarized growth and cytokinesis and rescued a defect in cell division induced by Bem3 misregulation. Collectively, our findings provide a potential molecular mechanism linking endocytosis (via epsin 2) with signaling pathways regulating cell division.

Indexed as

Cell DivisionEndocytosisSignal TransductionAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsCell PolarityChitin SynthaseCytokinesisGene Expression Regulation, FungalGenotypeGTPase-Activating ProteinsMiceMice, Inbred BALB CMolecular Sequence DataPhenotypeAdaptor Proteins, Vesicular TransportBEM3 protein, S cerevisiaeChitin SynthaseENT1 protein, S cerevisiaeENT2 protein, S cerevisiaeGTPase-Activating ProteinsSaccharomyces cerevisiae ProteinsVesicular Transport Proteins

Identifiers

PMID19531587
PMCPMC2704880
OpenAlexW2122391959

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.