EHD Proteins Associate with Syndapin I and II and Such Interactions Play a Crucial Role in Endosomal Recycling

• DOI: 10.1091/mbc.e05-01-0076
• Publication Date: 2005-06-02T00:25:48Z
• Authors: Anne Braun; Roser Pinyol; Regina Dahlhaus; Dennis Koch; Paul Fonarev; Barth D. Grant; Michael M. Kessels; Britta Qualmann
• Keywords: C2 domain; Transport protein; Cell fractionation

EHD proteins were shown to function in the exit of receptors and other membrane from endosomal recycling compartment. Here, we identify syndapins, accessory vesicle formation at plasma membrane, as differential binding partners for proteins. These complexes are formed by direct eps15-homology (EH) domain/asparagine proline phenylalanine (NPF) motif interactions. Heterologous endogenous coimmunoprecipitations well reconstitutions syndapin/EHD protein intracellular membranes living cells demonstrate vivo relevance interaction. The combination mutational analysis performed under different nucleotide conditions strongly suggest that modulates association with syndapins. Colocalization studies subcellular fractionation experiments support a role trafficking. Specific interferences syndapin–EHD interactions either overexpression isolated EHD-binding interface syndapin II or EHD1 EH domain inhibited transferrin suggesting domain/NPF critical recycling. Consistently, both inhibitions rescued co-overexpression attacked component. Our data thus reveal that, addition crucial endocytic internalization, play an important receptor