Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2006-2-1
pubmed:abstractText
Leukemia-associated fusion proteins establish aberrant transcriptional programs, which result in the block of hematopoietic differentiation, a prominent feature of the leukemic phenotype. The dissection of the mechanisms of deregulated transcription by leukemia fusion proteins is therefore critical for the design of tailored antileukemic strategies, aimed at reestablishing the differentiation program of leukemic cells. The acute promyelocytic leukemia (APL)-associated fusion protein PML-retinoic acid receptor (RAR) behaves as an aberrant transcriptional repressor, due to its ability to induce chromatin modifications (histone deacetylation and DNA methylation) and silencing of PML-RAR target genes. Here, we indicate that the ultimate result of PML-RAR action is to impose a heterochromatin-like structure on its target genes, thereby establishing a permanent transcriptional silencing. This effect is mediated by the previously described association of PML-RAR with chromatin-modifying enzymes (histone deacetylases and DNA methyltransferases) and by recruitment of the histone methyltransferase SUV39H1, responsible for trimethylation of lysine 9 of histone H3.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-10029573, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-10779362, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-10882117, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-10882118, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-10949293, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-11242053, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-11242054, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-11331580, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-11420727, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-11704848, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-11834837, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-11893494, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-12563308, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-14585615, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-14660751, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-14690609, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-14690610, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-15171245, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-15467421, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-15851025, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-8394219, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-8623923, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-8639758, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-8890168, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-8993033, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-9353180, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-9426049, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-9448006, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449642-9486655
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Histone-Lysine N-Methyltransferase, http://linkedlifedata.com/resource/pubmed/chemical/Histones, http://linkedlifedata.com/resource/pubmed/chemical/Methyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Oncogene Proteins, Fusion, http://linkedlifedata.com/resource/pubmed/chemical/PML protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Protein Methyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SUV39H1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/histone methyltransferase, http://linkedlifedata.com/resource/pubmed/chemical/promyelocytic leukemia-retinoic...
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0270-7306
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1288-96
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:16449642-Cell Differentiation, pubmed-meshheading:16449642-DNA Methylation, pubmed-meshheading:16449642-Gene Silencing, pubmed-meshheading:16449642-Histone-Lysine N-Methyltransferase, pubmed-meshheading:16449642-Histones, pubmed-meshheading:16449642-Humans, pubmed-meshheading:16449642-Leukemia, Promyelocytic, Acute, pubmed-meshheading:16449642-Methylation, pubmed-meshheading:16449642-Methyltransferases, pubmed-meshheading:16449642-Models, Biological, pubmed-meshheading:16449642-Neoplasm Proteins, pubmed-meshheading:16449642-Nuclear Proteins, pubmed-meshheading:16449642-Oncogene Proteins, Fusion, pubmed-meshheading:16449642-Protein Methyltransferases, pubmed-meshheading:16449642-Repressor Proteins, pubmed-meshheading:16449642-Transcription, Genetic, pubmed-meshheading:16449642-Transcription Factors, pubmed-meshheading:16449642-Transfection, pubmed-meshheading:16449642-Tumor Suppressor Proteins, pubmed-meshheading:16449642-U937 Cells
pubmed:year
2006
pubmed:articleTitle
Recruitment of the histone methyltransferase SUV39H1 and its role in the oncogenic properties of the leukemia-associated PML-retinoic acid receptor fusion protein.
pubmed:affiliation
Department of Experimental Oncology, European Institute of Oncology, and Department of Biomolecular Sciences and Biotechnologies, University of Milan, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't