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© The Rockefeller University Press, 0021-9525/2000//537 $5.00
The Journal of Cell Biology, Volume 149, Number 3, , 2000 537-546

Brief Report

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)



Joel Hymana,c, Hong Chenb,c, Pier Paolo Di Fiored, Pietro De Camillib,c, and Axel T. Brungera,c

a Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520
b Department of Cell Biology, Yale University, New Haven, Connecticut 06520
c Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06520
d Department of Experimental Oncology, European Institute of Oncology, Milan, Italy
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520.(203) 432-6946(203) 432-6143

brunger{at}laplace.csb.yale.edu

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.

Key Words: clathrin • Eps15 homology domain • catenin • karyopherin • endocytosis

© 2000 The Rockefeller University Press

Joel Hyman and Hong Chen contributed equally to this work.

The coordinates and structure factors have been deposited with the Research Collaboratory for Structural Bioinformatics (RSCB), accession number 1edu, and will also be available at http://atb.csb.yale.edu

Abbreviations used in this paper: CNS, Crystallography & NMR System; EH, Eps15 homology; ENTH domain, epsin NH2-terminal homology domain; epsin, Eps15 interactor; MAD, multiwavelength anomalous dispersion; NPF motifs, asparagine-proline-phenylalanine motifs; PLZF, promyelocytic leukemia Zn2+ finger protein; RMSD, root mean square difference; SeMet, selenomethionine.


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J. Cell Biol. 2000 149: 1-2. [Full Text] [PDF]





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