A snapshot of the physical and functional wiring of the Eps15 homology domain network in the nematode

Hanako Tsushima; Maria Grazia Malabarba; Stefano Confalonieri; Francesca Senic-Matuglia; Lisette G G C Verhoef; Cristina Bartocci; Giovanni D'Ario; Andrea Cocito; Pier Paolo Di Fiore; Anna Elisabetta Salcini

doi:10.1371/journal.pone.0056383

A snapshot of the physical and functional wiring of the Eps15 homology domain network in the nematode

Hanako Tsushima, Maria Grazia Malabarba, Stefano Confalonieri, Francesca Senic-Matuglia, Lisette G G C Verhoef, Cristina Bartocci, Giovanni D'Ario, Andrea Cocito, Pier Paolo Di Fiore, Anna Elisabetta Salcini

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Abstract

Protein interaction modules coordinate the connections within and the activity of intracellular signaling networks. The Eps15 Homology (EH) module, a protein-protein interaction domain that is a key feature of the EH-network, was originally identified in a few proteins involved in endocytosis and vesicle trafficking, and has subsequently also been implicated in actin reorganization, nuclear shuttling, and DNA repair. Here we report an extensive characterization of the physical connections and of the functional wirings of the EH-network in the nematode. Our data show that one of the major physiological roles of the EH-network is in neurotransmission. In addition, we found that the proteins of the network intersect, and possibly coordinate, a number of "territories" of cellular activity including endocytosis/recycling/vesicle transport, actin dynamics, general metabolism and signal transduction, ubiquitination/degradation of proteins, DNA replication/repair, and miRNA biogenesis and processing.

Original language	English
Journal	PloS one
Volume	8
Issue number	2
Pages (from-to)	e56383
ISSN	1932-6203
DOIs	https://doi.org/10.1371/journal.pone.0056383
Publication status	Published - 12 Feb 2013

Keywords

Adaptor Proteins, Vesicular Transport
Animals
Caenorhabditis elegans
Caenorhabditis elegans Proteins
Gene Expression Regulation
Protein Structure, Tertiary
Reproducibility of Results
Synaptic Transmission
Two-Hybrid System Techniques

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PLoS One 2013-8(2)-e56383. doi 10.1371Final published version, 767 KB

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Cite this

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title = "A snapshot of the physical and functional wiring of the Eps15 homology domain network in the nematode",

abstract = "Protein interaction modules coordinate the connections within and the activity of intracellular signaling networks. The Eps15 Homology (EH) module, a protein-protein interaction domain that is a key feature of the EH-network, was originally identified in a few proteins involved in endocytosis and vesicle trafficking, and has subsequently also been implicated in actin reorganization, nuclear shuttling, and DNA repair. Here we report an extensive characterization of the physical connections and of the functional wirings of the EH-network in the nematode. Our data show that one of the major physiological roles of the EH-network is in neurotransmission. In addition, we found that the proteins of the network intersect, and possibly coordinate, a number of {"}territories{"} of cellular activity including endocytosis/recycling/vesicle transport, actin dynamics, general metabolism and signal transduction, ubiquitination/degradation of proteins, DNA replication/repair, and miRNA biogenesis and processing.",

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AU - Tsushima, Hanako

AU - Malabarba, Maria Grazia

AU - Confalonieri, Stefano

AU - Senic-Matuglia, Francesca

AU - Verhoef, Lisette G G C

AU - Bartocci, Cristina

AU - D'Ario, Giovanni

AU - Cocito, Andrea

AU - Di Fiore, Pier Paolo

AU - Salcini, Anna Elisabetta

PY - 2013/2/12

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N2 - Protein interaction modules coordinate the connections within and the activity of intracellular signaling networks. The Eps15 Homology (EH) module, a protein-protein interaction domain that is a key feature of the EH-network, was originally identified in a few proteins involved in endocytosis and vesicle trafficking, and has subsequently also been implicated in actin reorganization, nuclear shuttling, and DNA repair. Here we report an extensive characterization of the physical connections and of the functional wirings of the EH-network in the nematode. Our data show that one of the major physiological roles of the EH-network is in neurotransmission. In addition, we found that the proteins of the network intersect, and possibly coordinate, a number of "territories" of cellular activity including endocytosis/recycling/vesicle transport, actin dynamics, general metabolism and signal transduction, ubiquitination/degradation of proteins, DNA replication/repair, and miRNA biogenesis and processing.

AB - Protein interaction modules coordinate the connections within and the activity of intracellular signaling networks. The Eps15 Homology (EH) module, a protein-protein interaction domain that is a key feature of the EH-network, was originally identified in a few proteins involved in endocytosis and vesicle trafficking, and has subsequently also been implicated in actin reorganization, nuclear shuttling, and DNA repair. Here we report an extensive characterization of the physical connections and of the functional wirings of the EH-network in the nematode. Our data show that one of the major physiological roles of the EH-network is in neurotransmission. In addition, we found that the proteins of the network intersect, and possibly coordinate, a number of "territories" of cellular activity including endocytosis/recycling/vesicle transport, actin dynamics, general metabolism and signal transduction, ubiquitination/degradation of proteins, DNA replication/repair, and miRNA biogenesis and processing.

KW - Adaptor Proteins, Vesicular Transport

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KW - Caenorhabditis elegans

KW - Caenorhabditis elegans Proteins

KW - Gene Expression Regulation

KW - Protein Structure, Tertiary

KW - Reproducibility of Results

KW - Synaptic Transmission

KW - Two-Hybrid System Techniques

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DO - 10.1371/journal.pone.0056383

M3 - Journal article

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SP - e56383

JO - PloS one

JF - PloS one

IS - 2

ER -

A snapshot of the physical and functional wiring of the Eps15 homology domain network in the nematode

Abstract

Keywords

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