15923258

Source:http://linkedlifedata.com/resource/pubmed/id/15923258

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0017262, umls-concept:C0019643, umls-concept:C0031715, umls-concept:C0185117, umls-concept:C0430054, umls-concept:C0456387, umls-concept:C1705053, umls-concept:C1709060, umls-concept:C2911684
pubmed:issue	23
pubmed:dateCreated	2005-6-8
pubmed:abstractText	Class II histone deacetylases (HDACs) repress transcription by associating with a variety of transcription factors and corepressors. Phosphorylation of a set of conserved serine residues in the N-terminal extensions of class II HDACs creates binding sites for 14-3-3 chaperone proteins, which trigger nuclear export of these HDACs, thereby derepressing specific target genes in a signal-dependent manner. To identify intracellular signaling pathways that control phosphorylation of HDAC5, a class II HDAC, we designed a eukaryotic cDNA expression screen in which a GAL4-dependent luciferase reporter was expressed with the DNA-binding domain of GAL4 fused to the N-terminal extension of HDAC5 and the VP16 transcription activation domain fused to 14-3-3. The transfection of COS cells with cDNA expression libraries results in activation of luciferase expression by cDNAs encoding HDAC5 kinases or modulators of such kinases that enable phosphorylated GAL4-HDAC5 to recruit 14-3-3-VP16 with consequent reconstitution of a functional transcriptional complex. Our results reveal a remarkable variety of signaling pathways that converge on the signal-responsive phosphorylation sites in HDAC5, thereby enabling HDAC5 to connect extracellular signals to the genome.
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pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/7505876
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary, http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylases, http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/rho GTP-Binding Proteins
pubmed:status	MEDLINE
pubmed:month	Jun
pubmed:issn	0027-8424
pubmed:author	pubmed-author:BezprozvannayaSvetlanaS, pubmed-author:ChangShurongS, pubmed-author:LiShijieS, pubmed-author:OlsonEric NEN
pubmed:issnType	Print
pubmed:day	7
pubmed:volume	102
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	8120-5
pubmed:dateRevised	2009-11-19
pubmed:meshHeading	pubmed-meshheading:15923258-Animals, pubmed-meshheading:15923258-COS Cells, pubmed-meshheading:15923258-Cloning, Molecular, pubmed-meshheading:15923258-DNA, Complementary, pubmed-meshheading:15923258-Gene Library, pubmed-meshheading:15923258-Histone Deacetylases, pubmed-meshheading:15923258-Humans, pubmed-meshheading:15923258-Mice, pubmed-meshheading:15923258-Phosphorylation, pubmed-meshheading:15923258-Protein Kinases, pubmed-meshheading:15923258-Receptors, Cell Surface, pubmed-meshheading:15923258-Signal Transduction, pubmed-meshheading:15923258-Transcription Factors, pubmed-meshheading:15923258-rho GTP-Binding Proteins
pubmed:year	2005
pubmed:articleTitle	An expression screen reveals modulators of class II histone deacetylase phosphorylation.
pubmed:affiliation	Department of Molecular Biology, University of Texas Southwestern Medical Center, 6000 Harry Hines Boulevard, Dallas, TX 75390, USA.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't