Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1999-7-6
pubmed:abstractText
In this paper we show that transcription factors Ets-1 and Ets-2 recruit transcription adapter proteins p300 and CBP (cAMP-responsive element-binding protein) during the transcriptional activation of the human stromelysin promoter, which contains palindromic Ets-binding sites. Ets-2 and p300/CBP exist as a complex in vivo. Two regions of p300/CBP between amino acids (a.a.) 328 and 596 and a. a. 1678 and 2370 independently can interact with Ets-1 and Ets-2 in vitro and in vivo. Both these regions of p300/CBP bind to the transactivation domain of Ets-2, whereas the C-terminal region binds only to the DNA binding domain of Ets-2. The N- and the C-terminal regions of CBP (a.a. 1-1097 and 1678-2442, respectively) which lack histone acetylation activity independently are capable of coactivating Ets-2. Other Ets family transcription factors failed to cooperate with p300/CBP in stimulating the stromelysin promoter. The LXXLL sequence, reported to be important in receptor-coactivator interactions, does not appear to play a role in the interaction of Ets-2 with p300/CBP. Previous studies have shown that the stimulation of transcriptional activation activity of Ets-2 requires phosphorylation of threonine 72 by the Ras/mitogen-activated protein kinase signaling pathway. We show that mutation of this site does not affect its capacity to bind to and to cooperate with p300/CBP.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/CREB-Binding Protein, http://linkedlifedata.com/resource/pubmed/chemical/CREBBP protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent..., http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/ERF protein, human, http://linkedlifedata.com/resource/pubmed/chemical/ERG protein, human, http://linkedlifedata.com/resource/pubmed/chemical/ETS1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/ETS2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 3, http://linkedlifedata.com/resource/pubmed/chemical/NCOA3 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Receptor Coactivator 3, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Protein c-ets-1, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Protein c-ets-2, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-ets, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/transcription factor PEA3
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
274
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
17342-52
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10358095-Binding Sites, pubmed-meshheading:10358095-CREB-Binding Protein, pubmed-meshheading:10358095-Calcium-Calmodulin-Dependent Protein Kinases, pubmed-meshheading:10358095-DNA-Binding Proteins, pubmed-meshheading:10358095-Histone Acetyltransferases, pubmed-meshheading:10358095-Humans, pubmed-meshheading:10358095-Matrix Metalloproteinase 3, pubmed-meshheading:10358095-Mutation, pubmed-meshheading:10358095-Nuclear Proteins, pubmed-meshheading:10358095-Nuclear Receptor Coactivator 3, pubmed-meshheading:10358095-Precipitin Tests, pubmed-meshheading:10358095-Promoter Regions, Genetic, pubmed-meshheading:10358095-Protein Binding, pubmed-meshheading:10358095-Proto-Oncogene Protein c-ets-1, pubmed-meshheading:10358095-Proto-Oncogene Protein c-ets-2, pubmed-meshheading:10358095-Proto-Oncogene Proteins, pubmed-meshheading:10358095-Proto-Oncogene Proteins c-ets, pubmed-meshheading:10358095-Repressor Proteins, pubmed-meshheading:10358095-Trans-Activators, pubmed-meshheading:10358095-Transcription Factors, pubmed-meshheading:10358095-Transcriptional Activation
pubmed:year
1999
pubmed:articleTitle
p300/cAMP-responsive element-binding protein interactions with ets-1 and ets-2 in the transcriptional activation of the human stromelysin promoter.
pubmed:affiliation
Lurie Cancer Center and Microbiology and Immunology Department, Northwestern University Medical School, Chicago, Illinois 60611, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't