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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
29
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pubmed:dateCreated |
2002-7-15
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pubmed:abstractText |
The ubiquitin-protein ligase EDD encodes an orthologue of the hyperplastic discs tumor suppressor gene, which has a critical role in Drosophila development. Frequent allelic imbalance at the EDD chromosomal locus in human cancers suggests a role in tumorigenesis. In addition to a HECT (homologous to E6-AP carboxyl terminus) domain, the EDD protein contains a UBR1 zinc finger motif and ubiquitin-associated domain, each of which indicates involvement in ubiquitinylation pathways. This study shows that EDD interacts with importin alpha 5 through consensus basic nuclear localization signals and is localized in cell nuclei. EDD also binds progesterone receptor (PR) and potentiates progestin-mediated gene transactivation. This activity is comparable with that of the coactivator SRC-1, but, in contrast, the interaction between EDD and PR does not appear to involve an LXXLL receptor-binding motif. EDD also binds calcium- and integrin-binding protein/DNA-dependent protein kinase-interacting protein, a potential target of ubiquitin-mediated proteolysis, and an altered association is found between EDD and calcium- and integrin-binding protein/DNA-dependent protein kinase-interacting protein in response to DNA damage. The data presented here demonstrate a role for EDD in PR signaling but also suggest a link to cancer through DNA damage response pathways.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CIB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/KPNA1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Synthases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Progesterone,
http://linkedlifedata.com/resource/pubmed/chemical/UBR5 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/alpha Karyopherins
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
26468-78
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:12011095-Amino Acid Sequence,
pubmed-meshheading:12011095-Calcium-Binding Proteins,
pubmed-meshheading:12011095-Carrier Proteins,
pubmed-meshheading:12011095-Cell Line,
pubmed-meshheading:12011095-Cell Nucleus,
pubmed-meshheading:12011095-DNA Damage,
pubmed-meshheading:12011095-Humans,
pubmed-meshheading:12011095-Molecular Sequence Data,
pubmed-meshheading:12011095-Peptide Synthases,
pubmed-meshheading:12011095-Plasmids,
pubmed-meshheading:12011095-Protein Binding,
pubmed-meshheading:12011095-Receptors, Progesterone,
pubmed-meshheading:12011095-Transcriptional Activation,
pubmed-meshheading:12011095-Two-Hybrid System Techniques,
pubmed-meshheading:12011095-Ubiquitin-Protein Ligases,
pubmed-meshheading:12011095-alpha Karyopherins
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pubmed:year |
2002
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pubmed:articleTitle |
EDD, the human hyperplastic discs protein, has a role in progesterone receptor coactivation and potential involvement in DNA damage response.
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pubmed:affiliation |
Cancer Research Program, Garvan Institute of Medical Research, St Vincent's Hospital, 384 Victoria Street, Darlinghurst, New South Wales 2010, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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