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

Gaelle Spagnol, Calliste Reiling, Fabien Kieken, Steve Caplan, Paul L. Sorgen

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)263-267
Number of pages5
JournalBiomolecular NMR Assignments
Volume8
Issue number2
DOIs
StatePublished - Oct 1 2014

Keywords

  • EH domain
  • EHD3
  • Endocytic recycling
  • NPF-motif

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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