Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
2004-4-19
pubmed:abstractText
Terminal differentiation of hematopoietic cells follows a precisely orchestrated program of transcriptional regulatory events at the promoters of both lineage-specific and ubiquitous genes. Here we show that the transcription factor ATF2 is associated with the induction of granulocytic differentiation, and the molecular interaction of ATF2 with a tissue-specific coactivator activating signal cointegator-2 (ASC-2) potentiates the differentiation procedure. All-trans retinoic acid (RA) induced the phosphorylation and expression of ATF2 in the early and middle phase of granulocyte differentiation, respectively. The activation of granulocyte-specific gene expression is increased with the concerted action of another basic regionleucine zipper factor, CCAAT/enhancer-binding protein (C/EBPalpha), and ASC-2, which function in a cooperative manner. The interaction between ATF2 and C/EBPalpha in RA-treated cells was enhanced by the ectopic expression of ASC-2. ATF2-mediated transactivation was also increased by co-transfection of ASC-2. This resulted from the direct protein interaction that the N-terminal transactivation domain of ATF2 interacts with the central region of ASC-2. Furthermore, the molecular interaction of ATF2 and ASC-2 was stimulated by RA treatment and inhibited by p38beta kinase inhibitor. Taking these results together, these results suggest that the differentiation-dependent expression and phosphorylation of ATF2 protein physically and functionally interacts with C/EBPalpha and coativator ASC-2 and synergizes to induce target gene transcription during granulocytic differentiation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/ATF2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Activating Transcription Factor 2, http://linkedlifedata.com/resource/pubmed/chemical/CCAAT-Enhancer-Binding Protein-alpha, http://linkedlifedata.com/resource/pubmed/chemical/Chromatin, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP Response..., http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase, http://linkedlifedata.com/resource/pubmed/chemical/Luciferases, http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 11, http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/Tretinoin
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
16996-7003
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:14734562-Activating Transcription Factor 2, pubmed-meshheading:14734562-Amino Acid Motifs, pubmed-meshheading:14734562-Blotting, Western, pubmed-meshheading:14734562-CCAAT-Enhancer-Binding Protein-alpha, pubmed-meshheading:14734562-Cell Differentiation, pubmed-meshheading:14734562-Cell Line, pubmed-meshheading:14734562-Cell Lineage, pubmed-meshheading:14734562-Chromatin, pubmed-meshheading:14734562-Cyclic AMP Response Element-Binding Protein, pubmed-meshheading:14734562-Dose-Response Relationship, Drug, pubmed-meshheading:14734562-Enzyme Inhibitors, pubmed-meshheading:14734562-Genes, Dominant, pubmed-meshheading:14734562-Glutathione Transferase, pubmed-meshheading:14734562-Granulocytes, pubmed-meshheading:14734562-HeLa Cells, pubmed-meshheading:14734562-Humans, pubmed-meshheading:14734562-Luciferases, pubmed-meshheading:14734562-Mitogen-Activated Protein Kinase 11, pubmed-meshheading:14734562-Mitogen-Activated Protein Kinases, pubmed-meshheading:14734562-Mutation, pubmed-meshheading:14734562-Phosphorylation, pubmed-meshheading:14734562-Precipitin Tests, pubmed-meshheading:14734562-Protein Binding, pubmed-meshheading:14734562-Protein Structure, Tertiary, pubmed-meshheading:14734562-Time Factors, pubmed-meshheading:14734562-Transcription, Genetic, pubmed-meshheading:14734562-Transcription Factors, pubmed-meshheading:14734562-Transcriptional Activation, pubmed-meshheading:14734562-Transfection, pubmed-meshheading:14734562-Tretinoin, pubmed-meshheading:14734562-Two-Hybrid System Techniques, pubmed-meshheading:14734562-U937 Cells
pubmed:year
2004
pubmed:articleTitle
Activation and interaction of ATF2 with the coactivator ASC-2 are responsive for granulocytic differentiation by retinoic acid.
pubmed:affiliation
Department of Molecular Biology, College of Natural Sciences, Pusan National University, Busan 609-735, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't