Epsin 1 Undergoes Nucleocytosolic Shuttling and Its Eps15 Interactor Nh2-Terminal Homology (Enth) Domain, Structurally Similar to Armadillo and Heat Repeats, Interacts with the Transcription Factor Promyelocytic Leukemia Zn2+ Finger Protein (Plzf)
Copyright policy )Epsin 1 Undergoes Nucleocytosolic Shuttling and Its Eps15 Interactor Nh2-Terminal Homology (Enth) Domain, Structurally Similar to Armadillo and Heat Repeats, Interacts with the Transcription Factor Promyelocytic Leukemia Zn2+ Finger Protein (Plzf)
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 NH2-terminal portion of epsin contains a phylogenetically conserved module of unknown function, known as the ENTH domain (epsin NH2-terminal homology domain). We have now solved the crystal structure of rat epsin 1 ENTH domain to 1.8 Å resolution. This domain is structurally similar to armadillo and Heat repeats of β-catenin and karyopherin-β, respectively. We have also identified and characterized the interaction of epsin 1, via the ENTH domain, with the transcription factor promyelocytic leukemia Zn2+ 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.
- Yale University United States
- University of Milan Italy
- European Institute of Oncology Italy
- Howard Hughes Medical Institute United States
Armadillo Domain Proteins, Cell Nucleus, Models, Molecular, Calcium-Binding Proteins, Molecular Sequence Data, Neuropeptides, Fluorescent Antibody Technique, Crystallography, X-Ray, Phosphoproteins, Cell Line, DNA-Binding Proteins, Adaptor Proteins, Vesicular Transport, Cytoskeletal Proteins, Cytosol, 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, Animals, Drosophila Proteins, Insect Proteins, Amino Acid Sequence, Carrier Proteins, Protein Binding
Armadillo Domain Proteins, Cell Nucleus, Models, Molecular, Calcium-Binding Proteins, Molecular Sequence Data, Neuropeptides, Fluorescent Antibody Technique, Crystallography, X-Ray, Phosphoproteins, Cell Line, DNA-Binding Proteins, Adaptor Proteins, Vesicular Transport, Cytoskeletal Proteins, Cytosol, 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, Animals, Drosophila Proteins, Insect Proteins, Amino Acid Sequence, Carrier Proteins, Protein Binding
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