Epsin 1 Undergoes Nucleocytosolic Shuttling and Its Eps15 Interactor Nh2-Terminal Homology (Enth) Domain, Structurally Similar to <i>Armadillo</i> and Heat Repeats, Interacts with the Transcription Factor Promyelocytic Leukemia Zn2+ Finger Protein (Plzf)
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- Joel Hyman
- aDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520
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- Hong Chen
- bDepartment of Cell Biology, Yale University, New Haven, Connecticut 06520
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- Pier Paolo Di Fiore
- dDepartment of Experimental Oncology, European Institute of Oncology, Milan, Italy
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- Pietro De Camilli
- bDepartment of Cell Biology, Yale University, New Haven, Connecticut 06520
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- Axel T. Brunger
- aDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520
抄録
<jats:p>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.</jats:p>
収録刊行物
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- The Journal of Cell Biology
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The Journal of Cell Biology 149 (3), 537-546, 2000-05-01
Rockefeller University Press