Linked Life Data

15588942

Source:http://linkedlifedata.com/resource/pubmed/id/15588942

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2004-12-13
pubmed:abstractText
CCAAT-enhancer binding protein-epsilon (C/EBPepsilon) is a nuclear transcription factor implicated in the regulation of terminal myeloid differentiation. Using a yeast two-hybrid screen, potential interaction partners of C/EBPepsilon involved in myeloid development were identified. C/EBPepsilon was found to associate with other C/EBP family members, including C/EBPepsilon and CHOP as well as other proteins that are known to contain a leucine-zipper protein interaction motif including CREB2, LDOC1, E6TP1, and AF-17. In addition, C/EBPepsilon demonstrated the potential for interaction with proteins that do not possess a leucine-zipper motif, including proteins that may be involved in sumoylation (protein inhibitor of activated STAT1 [PIAS1] and ubiquitin-conjugating enzyme E2I). As expected, the association of C/EBPepsilon with other C/EBP family members depends on the presence of a functional leucine-zipper motif. Mapping studies of C/EBPepsilon with PIAS1 (as an example of a nonleucine-zipper-containing protein) showed that C/EBPepsilon interacts with the amino-terminal domain of PIAS1. The function of C/EBPepsilon interacting proteins was further investigated. Co-expression of C/EBPepsilon with C/EBPdelta resulted in potent transactivation in a lactoferrin reporter system. A gel mobility shift assay suggests that C/EBPepsilon, C/EBPalpha, and C/EBPdelta proteins can bind as heterodimers to a C/EBP consensus DNA-binding site. As CHOP is known to represent a transcriptional repressor, the functional interaction between C/EBPepsilon and CHOP was investigated. Co-expression of C/EBPepsilon and c-Myb with CHOP caused marked transcriptional repression of target reporter genes. Our results suggest heterodimeric partners of C/EBPepsilon modulate the function of C/EBPepsilon in mediating gene transcription during myelopoiesis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0301-472X
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1173-81
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:15588942-CCAAT-Enhancer-Binding Proteins, pubmed-meshheading:15588942-Cell Differentiation, pubmed-meshheading:15588942-Electrophoretic Mobility Shift Assay, pubmed-meshheading:15588942-Gene Expression Regulation, pubmed-meshheading:15588942-Genes, Reporter, pubmed-meshheading:15588942-Humans, pubmed-meshheading:15588942-Jurkat Cells, pubmed-meshheading:15588942-Lactoferrin, pubmed-meshheading:15588942-Myelopoiesis, pubmed-meshheading:15588942-Protein Binding, pubmed-meshheading:15588942-Protein Inhibitors of Activated STAT, pubmed-meshheading:15588942-Protein Structure, Tertiary, pubmed-meshheading:15588942-Signal Transduction, pubmed-meshheading:15588942-Small Ubiquitin-Related Modifier Proteins, pubmed-meshheading:15588942-Transcription Factors, pubmed-meshheading:15588942-Ubiquitin-Conjugating Enzymes
pubmed:year
2004
pubmed:articleTitle
Protein partners of C/EBPepsilon.
pubmed:affiliation
Division of Hematology/Oncology, Cedars-Sinai Medical Center, UCLA School of Medicine, Los Angeles, Calif. 90048, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't