Literature DB >> 23754701

Chemical shift assignments of the C-terminal Eps15 homology domain-3 EH domain.

Gaelle Spagnol1, Calliste Reiling1, Fabien Kieken1, Steve Caplan1, Paul L Sorgen1.   

Abstract

The C-terminal Eps15 homology (EH) domain 3 (EHD3) belongs to a eukaryotic family of endocytic regulatory proteins and is involved in the recycling of various receptors from the early endosome to the endocytic recycling compartment or in retrograde transport from the endosomes to the Golgi. EH domains are highly conserved in the EHD family and function as protein-protein interaction units that bind to Asn-Pro-Phe (NPF) motif-containing proteins. The EH domain of EHD1 was the first C-terminal EH domain from the EHD family to be solved by NMR. The differences observed between this domain and proteins with N-terminal EH domains helped describe a mechanism for the differential binding of NPF-containing proteins. Here, structural studies were expanded to include the EHD3 EH domain. While the EHD1 and EHD3 EH domains are highly homologous, they have different protein partners. A comparison of these structures will help determine the selectivity in protein binding between the EHD family members and lead to a better understanding of their unique roles in endocytic regulation.

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Year:  2013        PMID: 23754701      PMCID: PMC3883950          DOI: 10.1007/s12104-013-9497-z

Source DB:  PubMed          Journal:  Biomol NMR Assign        ISSN: 1874-270X            Impact factor:   0.746


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