These findings shed new light on how EHD proteins selectively interact with specific NPF-containing partners that are involved in endocytic transport, and provide a means to identify potential new binding partners.

The EH domain is responsible for promoting specificity of interaction between the EHD protein and its associated effector. Current research suggests that the EH domain interacts with the NPF motif, a basic region classified by its arginine (N), proline (P), and phenylalanine (F) constituents.

Analysis of EHD/RME-1 family function, including its interactions with important protein and lipid partners, is providing new insights into the mechanisms that promote recycling within the endosomal system.

EHD proteins are characterized by an amino-terminal ATPase domain as well as a carboxyl-terminal EH domain; the EH domain is an EF hand-like structure that interacts with proteins containing an asparagine-proline-phenylalanine (NPF) motif (24 – 27).

In this review, we shall summa-rize the roles of the four EHD proteins and tabulate their known interaction partners. Although the review will focus primarily on mammalian EHDs, we shall also provide in-formation on the known functions of EHD proteins in model systems (Box 1).

Apr 15, 2015 · In this study, we sought to define the precise role of each PF motif in EHD2’s homo-dimerization, binding with the protein partners, and subcellular localization. To test the role of the NPF motif, we generated an EHD2 NPF-to-NAF mutant to mimic the homologous sequences of EHD1 and EHD3.

These findings shed new light on how EHD proteins selectively interact with specific NPF-containing partners that are involved in endocytic transport, and provide a means to identify potential new binding partners.

Apr 24, 2012 · In addition to binding EHD through the asparagine-proline-phenylalanine (NPF) motif found in its proline-rich domain (PRD), amphiphysin also binds the PRD of dynamin through its Src homology 3 (SH3) domain and can positively regulate vesicle formation in lampreys .

Nov 1, 2010 · At the N terminus, the EHD proteins contain a nucleotide-binding consensus site whereas at the C-terminus, they have an EF-hand calciumbinding EHD domain which interacts with proteins through...

EH-domain binding to proteins containing the tripeptide NPF has been well characterized, but recent studies have shown that EH-domains are also able to interact with ligands containing DPF or GPF motifs.