Epsin (Eps15 interactor) is a cytosolic protein involved in clathrin-mediated endocytosis via its direct interactions with clathrin, the clathrin adaptor AP-2, and Eps15. The NH(2)-terminal portion of epsin contains a phylogenetically conserved module of unknown function, known as the ENTH domain (epsin NH(2)-terminal homology domain). We have now solved the crystal structure of rat epsin 1 ENTH domain to 1.8 A resolution. This domain is structurally similar to armadillo and Heat repeats of beta-catenin and karyopherin-beta, respectively. We have also identified and characterized the interaction of epsin 1, via the ENTH domain, with the transcription factor promyelocytic leukemia Zn(2)+ finger protein (PLZF). Leptomycin B, an antifungal antibiotic, which inhibits the Crm1- dependent nuclear export pathway, induces an accumulation of epsin 1 in the nucleus. These findings suggest that epsin 1 may function in a signaling pathway connecting the endocytic machinery to the regulation of nuclear function.
|Titolo:||Epsin 1 undergoes nucleocytosolic shuttling and its eps15 interactor NH(2)-terminal homology (ENTH) domain, structurally similar to Armadillo and HEAT repeats, interacts with the transcription factor promyelocytic leukemia Zn(2)+ finger protein (PLZF)|
|Parole Chiave:||Animals; Rats; Calcium-Binding Proteins; Phosphoproteins; Sequence Alignment; Transcription Factors; Drosophila Proteins; Molecular Sequence Data; Cytoskeletal Proteins; Trans-Activators; Fluorescent Antibody Technique; Neuropeptides; Carrier Proteins; Models, Molecular; DNA-Binding Proteins; Insect Proteins; beta Catenin; Vesicular Transport Proteins; Amino Acid Sequence; Cell Nucleus; Protein Binding; Adaptor Proteins, Vesicular Transport; Cytosol; Zinc Fingers; Crystallography, X-Ray; Armadillo Domain Proteins; Cell Line|
|Settore Scientifico Disciplinare:||Settore MED/04 - Patologia Generale|
|Data di pubblicazione:||1-mag-2000|
|Digital Object Identifier (DOI):||10.1083/jcb.149.3.537|
|Appare nelle tipologie:||01 - Articolo su periodico|