C-terminal EH-domain-containing proteins

Consensus for a role in endocytic trafficking, EH?

Research output: Contribution to journalComment/debate

76 Citations (Scopus)

Abstract

The Eps15-homology (EH) domain is a highly conserved motif comprising ∼100 residues that is found in proteins from species as diverse as yeast and mammals. Proteins that have an EH domain can carry out a variety of crucial cellular functions ranging from regulation of the actin cytoskeleton, signal transduction and transcriptional regulation to control of the endocytic pathway. EH domains bind to proteins that contain the tripeptide asparagine-proline-phenylalanine (NPF). Although EH domains are typically found at the N-terminus, mammalian cells express four highly homologous C-terminal EH-domain-containing paralogs (EHD1-EHD4), which exhibit broad amino acid conservation throughout the entire sequence. These C-terminal EH-domain-containing proteins also contain a central coiled-coil region involved in oligomerization, as well as an N-terminal nucleotide-binding motif. Recent studies have identified an array of novel binding partners for EHD1-EHD4, including NPF-containing proteins, such as the divalent Rab4/5 effector rabenosyn 5, the cell fate determinant Numb, EH-binding protein 1 (EHBP1) and syndapins I and II. Interactions with the clathrin heavy-chain and components of the internalization machinery have also been described. Indeed, C-terminal EH-domain-containing proteins appear to regulate several key endocytic steps, including internalization and recycling. EHD1 and EHD4 control recycling by regulating the transport of receptors from the recycling compartment to the plasma membrane. EHD1, EHD2 and EHD4 have also been implicated in the internalization of receptors and their transport to early endosomes.

Original languageEnglish (US)
Pages (from-to)4093-4101
Number of pages9
JournalJournal of Cell Science
Volume118
Issue number18
DOIs
StatePublished - Sep 15 2005

Fingerprint

Recycling
Proteins
Clathrin Heavy Chains
Nucleotide Motifs
Asparagine
Endosomes
Phenylalanine
Actin Cytoskeleton
Proline
Mammals
Signal Transduction
Carrier Proteins
Yeasts
Cell Membrane
Amino Acids
Protein Domains

Keywords

  • Endocytosis
  • Eps15 homology (EH) domain
  • Recycling

ASJC Scopus subject areas

  • Cell Biology

Cite this

C-terminal EH-domain-containing proteins : Consensus for a role in endocytic trafficking, EH? / Naslavsky, Naava; Caplan, Steven H.

In: Journal of Cell Science, Vol. 118, No. 18, 15.09.2005, p. 4093-4101.

Research output: Contribution to journalComment/debate

@article{0421b0ef49884531ab5c1e61fb9c8eae,
title = "C-terminal EH-domain-containing proteins: Consensus for a role in endocytic trafficking, EH?",
abstract = "The Eps15-homology (EH) domain is a highly conserved motif comprising ∼100 residues that is found in proteins from species as diverse as yeast and mammals. Proteins that have an EH domain can carry out a variety of crucial cellular functions ranging from regulation of the actin cytoskeleton, signal transduction and transcriptional regulation to control of the endocytic pathway. EH domains bind to proteins that contain the tripeptide asparagine-proline-phenylalanine (NPF). Although EH domains are typically found at the N-terminus, mammalian cells express four highly homologous C-terminal EH-domain-containing paralogs (EHD1-EHD4), which exhibit broad amino acid conservation throughout the entire sequence. These C-terminal EH-domain-containing proteins also contain a central coiled-coil region involved in oligomerization, as well as an N-terminal nucleotide-binding motif. Recent studies have identified an array of novel binding partners for EHD1-EHD4, including NPF-containing proteins, such as the divalent Rab4/5 effector rabenosyn 5, the cell fate determinant Numb, EH-binding protein 1 (EHBP1) and syndapins I and II. Interactions with the clathrin heavy-chain and components of the internalization machinery have also been described. Indeed, C-terminal EH-domain-containing proteins appear to regulate several key endocytic steps, including internalization and recycling. EHD1 and EHD4 control recycling by regulating the transport of receptors from the recycling compartment to the plasma membrane. EHD1, EHD2 and EHD4 have also been implicated in the internalization of receptors and their transport to early endosomes.",
keywords = "Endocytosis, Eps15 homology (EH) domain, Recycling",
author = "Naava Naslavsky and Caplan, {Steven H}",
year = "2005",
month = "9",
day = "15",
doi = "10.1242/jcs.02595",
language = "English (US)",
volume = "118",
pages = "4093--4101",
journal = "Journal of Cell Science",
issn = "0021-9533",
publisher = "Company of Biologists Ltd",
number = "18",

}

TY - JOUR

T1 - C-terminal EH-domain-containing proteins

T2 - Consensus for a role in endocytic trafficking, EH?

AU - Naslavsky, Naava

AU - Caplan, Steven H

PY - 2005/9/15

Y1 - 2005/9/15

N2 - The Eps15-homology (EH) domain is a highly conserved motif comprising ∼100 residues that is found in proteins from species as diverse as yeast and mammals. Proteins that have an EH domain can carry out a variety of crucial cellular functions ranging from regulation of the actin cytoskeleton, signal transduction and transcriptional regulation to control of the endocytic pathway. EH domains bind to proteins that contain the tripeptide asparagine-proline-phenylalanine (NPF). Although EH domains are typically found at the N-terminus, mammalian cells express four highly homologous C-terminal EH-domain-containing paralogs (EHD1-EHD4), which exhibit broad amino acid conservation throughout the entire sequence. These C-terminal EH-domain-containing proteins also contain a central coiled-coil region involved in oligomerization, as well as an N-terminal nucleotide-binding motif. Recent studies have identified an array of novel binding partners for EHD1-EHD4, including NPF-containing proteins, such as the divalent Rab4/5 effector rabenosyn 5, the cell fate determinant Numb, EH-binding protein 1 (EHBP1) and syndapins I and II. Interactions with the clathrin heavy-chain and components of the internalization machinery have also been described. Indeed, C-terminal EH-domain-containing proteins appear to regulate several key endocytic steps, including internalization and recycling. EHD1 and EHD4 control recycling by regulating the transport of receptors from the recycling compartment to the plasma membrane. EHD1, EHD2 and EHD4 have also been implicated in the internalization of receptors and their transport to early endosomes.

AB - The Eps15-homology (EH) domain is a highly conserved motif comprising ∼100 residues that is found in proteins from species as diverse as yeast and mammals. Proteins that have an EH domain can carry out a variety of crucial cellular functions ranging from regulation of the actin cytoskeleton, signal transduction and transcriptional regulation to control of the endocytic pathway. EH domains bind to proteins that contain the tripeptide asparagine-proline-phenylalanine (NPF). Although EH domains are typically found at the N-terminus, mammalian cells express four highly homologous C-terminal EH-domain-containing paralogs (EHD1-EHD4), which exhibit broad amino acid conservation throughout the entire sequence. These C-terminal EH-domain-containing proteins also contain a central coiled-coil region involved in oligomerization, as well as an N-terminal nucleotide-binding motif. Recent studies have identified an array of novel binding partners for EHD1-EHD4, including NPF-containing proteins, such as the divalent Rab4/5 effector rabenosyn 5, the cell fate determinant Numb, EH-binding protein 1 (EHBP1) and syndapins I and II. Interactions with the clathrin heavy-chain and components of the internalization machinery have also been described. Indeed, C-terminal EH-domain-containing proteins appear to regulate several key endocytic steps, including internalization and recycling. EHD1 and EHD4 control recycling by regulating the transport of receptors from the recycling compartment to the plasma membrane. EHD1, EHD2 and EHD4 have also been implicated in the internalization of receptors and their transport to early endosomes.

KW - Endocytosis

KW - Eps15 homology (EH) domain

KW - Recycling

UR - http://www.scopus.com/inward/record.url?scp=27144515960&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=27144515960&partnerID=8YFLogxK

U2 - 10.1242/jcs.02595

DO - 10.1242/jcs.02595

M3 - Comment/debate

VL - 118

SP - 4093

EP - 4101

JO - Journal of Cell Science

JF - Journal of Cell Science

SN - 0021-9533

IS - 18

ER -