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)

Hyman, Joel; Chen, Hong; Di Fiore, Pier Paolo; De Camilli, Pietro; Brunger, Axel T.

doi:10.1083/jcb.149.3.537

Title: 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)

Journal Article · Mon May 01 00:00:00 EDT 2000 · Journal of Cell Biology

DOI:https://doi.org/10.1083/jcb.149.3.537· OSTI ID:1625117

Hyman, Joel ^[1]; Chen, Hong ^[2]; Di Fiore, Pier Paolo ^[3]; De Camilli, Pietro ^[4]; Brunger, Axel T. ^[1]

Yale Univ., New Haven, CT (United States). Dept. of Molecular Biophysics and Biochemistry; Yale Univ., New Haven, CT (United States) Howard Hughes Medical Inst.
Yale Univ., New Haven, CT (United States). Dept. of of Cell Biology; Yale Univ., New Haven, CT (United States). Howard Hughes Medical Inst.
European Inst. of Oncology, Milan (Italy). Dept. of Experimental Oncology
Yale Univ., New Haven, CT (United States). Dept. of of Cell Biology; Yale Univ., New Haven, CT (United States). Howard Hughes Medical Inst.

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.

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Research Organization:: Yale Univ., New Haven, CT (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division; National Institutes of Health (NIH)

Grant/Contract Number:: CA46128; NS36252

OSTI ID:: 1625117

Journal Information:: Journal of Cell Biology, Vol. 149, Issue 3; ISSN 0021-9525

Publisher:: Rockefeller University PressCopyright Statement

Country of Publication:: United States

Language:: English

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59 BASIC BIOLOGICAL SCIENCES
cell biology
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Title: 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)

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Title: 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)