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
·
· Journal of Cell Biology
- Yale Univ., New Haven, CT (United States). Dept. of Molecular Biophysics and Biochemistry; Yale Univ., New Haven, CT (United States) Howard Hughes Medical Inst.; DOE/OSTI
- 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.
- Yale Univ., New Haven, CT (United States). Dept. of Molecular Biophysics and Biochemistry; 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.
- Research Organization:
- Yale Univ., New Haven, CT (United States)
- Sponsoring Organization:
- National Institutes of Health (NIH); USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division
- OSTI ID:
- 1625117
- Journal Information:
- Journal of Cell Biology, Journal Name: Journal of Cell Biology Journal Issue: 3 Vol. 149; ISSN 0021-9525
- Publisher:
- Rockefeller University PressCopyright Statement
- Country of Publication:
- United States
- Language:
- English
Similar Records
Redox-mediated modification of PLZF by SUMO-1 and ubiquitin
PLZF-RAR[alpha] fusion proteins generated from the variant t(11; 17)(q23; q21) translocation in acute promyelocytic leukemia inhibit ligand-dependent transactivation of wild-type retinoic acid receptors
An Armadillo Motif in Ufd3 Interacts with Cdc48 and is Involved in Ubiquitin Homeostasis and Protein Degradation
Journal Article
·
Fri May 16 00:00:00 EDT 2008
· Biochemical and Biophysical Research Communications
·
OSTI ID:21143689
PLZF-RAR[alpha] fusion proteins generated from the variant t(11; 17)(q23; q21) translocation in acute promyelocytic leukemia inhibit ligand-dependent transactivation of wild-type retinoic acid receptors
Journal Article
·
Mon Jan 31 23:00:00 EST 1994
· Proceedings of the National Academy of Sciences of the United States of America; (United States)
·
OSTI ID:7009364
An Armadillo Motif in Ufd3 Interacts with Cdc48 and is Involved in Ubiquitin Homeostasis and Protein Degradation
Journal Article
·
Wed Dec 31 23:00:00 EST 2008
· Proceedings of the National Academy of Sciences of the United States of America
·
OSTI ID:980007