Evidence map›Paper›PMID 23553749›Full record

ArticleProtein science : a publication of the Protein Society2013

Crystallographic analysis of the ENTH domain from yeast epsin Ent2 that induces a cell division phenotype.

Gregory T Costakes, Arpita Sen, R Claudio Aguilar, Cynthia V Stauffacher

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2013. 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
0.2field-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

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3 · Its place in the literature

Who cites it

4 citing papers in PubMed, 5 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

4 authors at 2 institutions in 1 country.

Gregory T CostakesDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA.
Arpita Sen
R Claudio Aguilar
Cynthia V Stauffacher
Center for Cancer Research · USPurdue University West Lafayette · US

Funding

BIOPHYS STUD OF PROTEINS, NUCLEIC ACIDS, AND VIRUSEST32GM008296 · NIGMS · PURDUE UNIVERSITY WEST LAFAYETTE · PI STAUFFACHER, CYNTHIA VIANNE · 1989 to 2012
$2.2M
NIGMS NIH HHS T32 GM008296
6 · The paper itself

Abstract

Epsins are eukaryotic, endocytic adaptor proteins primarily involved in the early steps of clathrin mediated endocytosis. Two epsins exist in Saccharomyces cerevisiae, Ent1 and Ent2, with single epsin knockouts being viable, while the double knockout is not. These proteins contain a highly conserved Epsin N-terminal homology (ENTH) domain that is essential for cell viability. In addition, overexpression of the ENTH domain of Ent2 (ENTH2) was shown to play a role in cell division by interacting with the septin organizing, Cdc42 GTPase activating protein, Bem3, leading to increased cytokinesis failure. In contrast, overexpression of the ENTH domain of Ent1 (ENTH1) does not affect cytokinesis, despite being 75% identical to ENTH2. An ENTH2(N112D, S114E, E118Q) mutant that switches residues in loop 7 to those found correspondingly in ENTH1 was incapable of inducing the cytokinesis phenotype. In order to better understand the role of loop 7 in the ENTH2-induced phenotype at a molecular level, X-ray crystallography was used to elucidate the structures of yeast ENTH2(WT) and ENTH2(DEQ). Our results indicate that mutations did not affect the conformation of loop 7, but rather introduce an increased negative charge on a potential interaction interface. Morphological analysis of cells overexpressing ENTH2 loop 7 mutants showed that the cytokinesis failure phenotype was abolished by the single mutants N112D, E118Q, and to a lesser extent by S114E. Taken together, our results indicate that the interaction surface that contains loop 7 and the specific nature of these residues are crucial for ENTH2 involvement in cytokinesis. This research provides insight into a molecular mechanism by which ENTH2, but not ENTH1, overexpression in yeast leads to cell division defects. Structural data of WT and mutant ENTH2 domains along with in vivo phenotypic analysis of ENTH2 overexpressing cells indicate that the biochemical nature of three loop 7 residues is crucial for its role in cytokinesis.

Indexed as

Adaptor Proteins, Vesicular TransportCrystallography, X-RayModels, MolecularMutationProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUp-RegulationAdaptor Proteins, Vesicular TransportENT2 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID23553749
PMCPMC3690715
OpenAlexW2158513753

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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.