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PMID: 10791968 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Epsin 1 undergoes nucleocytosolic shuttling and its eps15 interactor NH(2)-terminal homology (ENTH) domain, structurally similar to Armadillo and HEAT repeats, interacts with the transcription factor promyelocytic leukemia Zn(2)+ finger protein (PLZF).

The Journal of cell biology ·Vol. 149 ·No. 3 ·2000-05-01 ·Pages 537-46

Hyman J, Chen H, Di Fiore PP, De Camilli P, Brunger AT

Abstract

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 NH(2)-terminal portion of epsin contains a phylogenetically conserved module of unknown function, known as the ENTH domain (epsin NH(2)-terminal homology domain). We have now solved the crystal structure of rat epsin 1 ENTH domain to 1.8 A resolution. This domain is structurally similar to armadillo and Heat repeats of beta-catenin and karyopherin-beta, respectively. We have also identified and characterized the interaction of epsin 1, via the ENTH domain, with the transcription factor promyelocytic leukemia Zn(2)+ 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.

MeSH Terms
Adaptor Proteins, Vesicular Transport Amino Acid Sequence Animals Armadillo Domain Proteins Calcium-Binding Proteins/metabolism Carrier Proteins/chemistry,metabolism Cell Line Cell Nucleus/metabolism Crystallography, X-Ray Cytoskeletal Proteins/chemistry Cytosol/metabolism DNA-Binding Proteins/metabolism Drosophila Proteins Fluorescent Antibody Technique Insect Proteins/chemistry Models, Molecular Molecular Sequence Data Neuropeptides/chemistry,metabolism Phosphoproteins/metabolism Protein Binding Rats Sequence Alignment Trans-Activators Transcription Factors/metabolism Vesicular Transport Proteins Zinc Fingers beta Catenin
Chemicals
Adaptor Proteins, Vesicular Transport Armadillo Domain Proteins Calcium-Binding Proteins Carrier Proteins Ctnnb1 protein, rat Cytoskeletal Proteins DNA-Binding Proteins Drosophila Proteins Insect Proteins Neuropeptides Phosphoproteins Trans-Activators Transcription Factors Vesicular Transport Proteins beta Catenin epsin
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Hyman J
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520, USA.
Chen H
Di Fiore P P
De Camilli P
Brunger A T
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
Published
2000-05-01
Pages
537-46
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2174850
Subset
IM
Grants
NCI NIH HHS · CA46128 · United States
NINDS NIH HHS · NS36252 · United States
Databases
PDB
Analysis Services
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