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C-terminal EH-domain-containing proteins: consensus for a role in endocytic trafficking, EH?

Naslavsky, Naava, Caplan, Steve·2005·Journal of Cell Science
DOI 10.1242/jcs.02595
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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.

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  • EHD1 binding to SNX17 is atypical because most of the EHD1 interaction partners identified to date interact via NPF motifs.

    “EHD1 binding to SNX17 is atypical because most of the EHD1 interaction partners identified to date interact via NPF motifs”

    From Sorting nexin 17 (SNX17) links endosomal sorting to Eps15 homology domain protein 1 (EHD1)–mediated fission machinery (2020) · cites this paper as [22]

  • EHD1 plays a critical role in recycling of plasma membrane receptors (e.g., transferrin) internalized through clathrin-coated pits or independently of clathrin.

    “EHD1 [14] has been found to play a critical role in the recycling of plasma membrane receptors (ie., transferrin) that are internalized either through clathrin-coated pits [15-17], or independently of clathrin (MHC-I or β1 integrins) [18,19].”

    From EHD1 regulates cholesterol homeostasis and lipid droplet storage (2007) · cites this paper as [16]

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Metadata

Authors
Naslavsky, N., & Caplan, S.
Affiliations
Department of Biochemistry and Molecular Biology and Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, NE 68198-5870, USA
Venue
Journal of Cell Science
Publisher
The Company of Biologists
Published
2005-09-15
Volume
118
Issue
18
Pages
4093-4101
ISSN
  • 1477-9137
  • 0021-9533
DOI
10.1242/jcs.02595
Cited by
98
References
2
Language
en

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