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)

doi:10.1083/jcb.149.3.537

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© The Rockefeller University Press, 0021-9525/2000/5/537/ $5.00
The Journal of Cell Biology, Volume 149, Number 3, May 1, 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 Hyman^a,c, Hong Chen^b,c, Pier Paolo Di Fiore^d, Pietro De Camilli^b,c, and Axel T. Brunger^a,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

Correspondence to: Axel T. Brunger, Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520. Tel:(203) 432-6143 Fax:(203) 432-6946 E-mail:brunger{at}laplace.csb.yale.edu.

Epsin (Eps15 interactor) is a cytosolic protein involved inclathrin-mediated endocytosis via its direct interactions withclathrin, the clathrin adaptor AP-2, and Eps15. The NH₂-terminalportion of epsin contains a phylogenetically conserved moduleof unknown function, known as the ENTH domain (epsin NH₂-terminalhomology domain). We have now solved the crystal structure ofrat epsin 1 ENTH domain to 1.8 Å resolution. This domainis structurally similar to armadillo and Heat repeats of ß-cateninand karyopherin-ß, respectively. We have also identifiedand characterized the interaction of epsin 1, via the ENTH domain,with the transcription factor promyelocytic leukemia Zn²+ fingerprotein (PLZF). Leptomycin B, an antifungal antibiotic, whichinhibits the Crm1- dependent nuclear export pathway, inducesan accumulation of epsin 1 in the nucleus. These findings suggestthat epsin 1 may function in a signaling pathway connectingthe endocytic machinery to the regulation of nuclear function.

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

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