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)

J Cell Biol. 2000 May 1;149(3):537-46. doi: 10.1083/jcb.149.3.537.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adaptor Proteins, Vesicular Transport
  • Amino Acid Sequence
  • Animals
  • Armadillo Domain Proteins
  • Calcium-Binding Proteins / metabolism*
  • Carrier Proteins / chemistry*
  • Carrier Proteins / 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*
  • Neuropeptides / metabolism
  • Phosphoproteins / metabolism*
  • Protein Binding
  • Rats
  • Sequence Alignment
  • Trans-Activators*
  • Transcription Factors / metabolism*
  • Vesicular Transport Proteins*
  • Zinc Fingers
  • beta Catenin

Substances

  • 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

Associated data

  • PDB/1EDU