EH and UIM: endocytosis and more.

Simona Polo, Stefano Confalonieri, Anna Elisabetta Salcini, Pier Paolo Di Fiore

Research output: Contribution to journalArticle

87 Citations (Scopus)

Abstract

Exogenously and endogenously originated signals are propagated within the cell by functional and physical networks of proteins, leading to numerous biological outcomes. Many protein-protein interactions take place between binding domains and short peptide motifs. Frequently, these interactions are inducible by upstream signaling events, in which case one of the two binding surfaces may be created by a posttranslational modification. Here, we discuss two protein networks. One, the EH-network, is based on the Eps15 homology (EH) domain, which binds to peptides containing the sequence Asp-Pro-Phe (NPF). The other, which we define as the monoubiquitin (mUb) network, relies on monoubiquitination, which is emerging as an important posttranslational modification that regulates protein function. Both networks were initially implicated in the control of plasma membrane receptor endocytosis and in the regulation of intracellular trafficking routes. The ramifications of these two networks, however, appear to extend into many other aspects of cell physiology as well, such as transcriptional regulation, actin cytoskeleton remodeling, and DNA repair. The focus of this review is to integrate available knowledge of the EH- and mUb networks with predictions of genetic and physical interactions stemming from functional genomics approaches.

Original languageEnglish
JournalScience's STKE : signal transduction knowledge environment
Volume2003
Issue number213
Publication statusPublished - 2003

Fingerprint

Endocytosis
Post Translational Protein Processing
Proteins
Cell Physiological Phenomena
Genomics
Actin Cytoskeleton
DNA Repair
Cell Membrane
Peptides

Cite this

EH and UIM : endocytosis and more. / Polo, Simona; Confalonieri, Stefano; Salcini, Anna Elisabetta; Di Fiore, Pier Paolo.

In: Science's STKE : signal transduction knowledge environment, Vol. 2003, No. 213, 2003.

Research output: Contribution to journalArticle

Polo, Simona ; Confalonieri, Stefano ; Salcini, Anna Elisabetta ; Di Fiore, Pier Paolo. / EH and UIM : endocytosis and more. In: Science's STKE : signal transduction knowledge environment. 2003 ; Vol. 2003, No. 213.
@article{186d40c635c94174bad71572aff6fbd4,
title = "EH and UIM: endocytosis and more.",
abstract = "Exogenously and endogenously originated signals are propagated within the cell by functional and physical networks of proteins, leading to numerous biological outcomes. Many protein-protein interactions take place between binding domains and short peptide motifs. Frequently, these interactions are inducible by upstream signaling events, in which case one of the two binding surfaces may be created by a posttranslational modification. Here, we discuss two protein networks. One, the EH-network, is based on the Eps15 homology (EH) domain, which binds to peptides containing the sequence Asp-Pro-Phe (NPF). The other, which we define as the monoubiquitin (mUb) network, relies on monoubiquitination, which is emerging as an important posttranslational modification that regulates protein function. Both networks were initially implicated in the control of plasma membrane receptor endocytosis and in the regulation of intracellular trafficking routes. The ramifications of these two networks, however, appear to extend into many other aspects of cell physiology as well, such as transcriptional regulation, actin cytoskeleton remodeling, and DNA repair. The focus of this review is to integrate available knowledge of the EH- and mUb networks with predictions of genetic and physical interactions stemming from functional genomics approaches.",
author = "Simona Polo and Stefano Confalonieri and Salcini, {Anna Elisabetta} and {Di Fiore}, {Pier Paolo}",
year = "2003",
language = "English",
volume = "2003",
journal = "Science's STKE : signal transduction knowledge environment",
issn = "1525-8882",
publisher = "American Association for the Advancement of Science",
number = "213",

}

TY - JOUR

T1 - EH and UIM

T2 - endocytosis and more.

AU - Polo, Simona

AU - Confalonieri, Stefano

AU - Salcini, Anna Elisabetta

AU - Di Fiore, Pier Paolo

PY - 2003

Y1 - 2003

N2 - Exogenously and endogenously originated signals are propagated within the cell by functional and physical networks of proteins, leading to numerous biological outcomes. Many protein-protein interactions take place between binding domains and short peptide motifs. Frequently, these interactions are inducible by upstream signaling events, in which case one of the two binding surfaces may be created by a posttranslational modification. Here, we discuss two protein networks. One, the EH-network, is based on the Eps15 homology (EH) domain, which binds to peptides containing the sequence Asp-Pro-Phe (NPF). The other, which we define as the monoubiquitin (mUb) network, relies on monoubiquitination, which is emerging as an important posttranslational modification that regulates protein function. Both networks were initially implicated in the control of plasma membrane receptor endocytosis and in the regulation of intracellular trafficking routes. The ramifications of these two networks, however, appear to extend into many other aspects of cell physiology as well, such as transcriptional regulation, actin cytoskeleton remodeling, and DNA repair. The focus of this review is to integrate available knowledge of the EH- and mUb networks with predictions of genetic and physical interactions stemming from functional genomics approaches.

AB - Exogenously and endogenously originated signals are propagated within the cell by functional and physical networks of proteins, leading to numerous biological outcomes. Many protein-protein interactions take place between binding domains and short peptide motifs. Frequently, these interactions are inducible by upstream signaling events, in which case one of the two binding surfaces may be created by a posttranslational modification. Here, we discuss two protein networks. One, the EH-network, is based on the Eps15 homology (EH) domain, which binds to peptides containing the sequence Asp-Pro-Phe (NPF). The other, which we define as the monoubiquitin (mUb) network, relies on monoubiquitination, which is emerging as an important posttranslational modification that regulates protein function. Both networks were initially implicated in the control of plasma membrane receptor endocytosis and in the regulation of intracellular trafficking routes. The ramifications of these two networks, however, appear to extend into many other aspects of cell physiology as well, such as transcriptional regulation, actin cytoskeleton remodeling, and DNA repair. The focus of this review is to integrate available knowledge of the EH- and mUb networks with predictions of genetic and physical interactions stemming from functional genomics approaches.

UR - http://www.scopus.com/inward/record.url?scp=1542674420&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=1542674420&partnerID=8YFLogxK

M3 - Article

C2 - 14679291

AN - SCOPUS:1542674420

VL - 2003

JO - Science's STKE : signal transduction knowledge environment

JF - Science's STKE : signal transduction knowledge environment

SN - 1525-8882

IS - 213

ER -