rdf:type |
|
lifeskim:mentions |
umls-concept:C0012933,
umls-concept:C0031715,
umls-concept:C0035678,
umls-concept:C0036720,
umls-concept:C0040649,
umls-concept:C1421307,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1704675,
umls-concept:C1879547
|
pubmed:issue |
24
|
pubmed:dateCreated |
2001-11-21
|
pubmed:abstractText |
Modulation of the activity of the upstream binding factor (UBF) plays a key role in cell cycle-dependent regulation of rRNA synthesis. Activation of rDNA transcription on serum stimulation requires phosphorylation of UBF at serine 484 by G(1)-specific cyclin-dependent kinase (cdk)/cyclin complexes. After G(1) progression UBF is phosphorylated at serine 388 by cdk2/cyclin E and cdk2/cyclin A. Conversion of serine 388 to glycine abolishes UBF activity, whereas substitution by aspartate enhances the transactivating function of UBF. Protein-protein interaction studies reveal that phosphorylation at serine 388 is required for the interaction between RNA polymerase I and UBF. The results suggest that phosphorylation of UBF represents a powerful means of modulating the assembly of the transcription initiation complex in a proliferation- and cell cycle-dependent fashion.
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11698641-10082553,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11698641-10202152,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11698641-10339547,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11698641-1561086,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11698641-1600946,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11698641-1730600,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11698641-4075406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11698641-4472266,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11698641-7491500,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11698641-7651819,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11698641-7877691,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11698641-8306961,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11698641-8552083,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11698641-8641287,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11698641-9017602,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11698641-9234680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11698641-9857193
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Nov
|
pubmed:issn |
0027-8424
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
20
|
pubmed:volume |
98
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
13631-6
|
pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11698641-3T3 Cells,
pubmed-meshheading:11698641-Animals,
pubmed-meshheading:11698641-Cell Cycle,
pubmed-meshheading:11698641-Cell Line,
pubmed-meshheading:11698641-DNA, Ribosomal,
pubmed-meshheading:11698641-DNA-Binding Proteins,
pubmed-meshheading:11698641-Mice,
pubmed-meshheading:11698641-Phosphorylation,
pubmed-meshheading:11698641-Pol1 Transcription Initiation Complex Proteins,
pubmed-meshheading:11698641-RNA Polymerase I,
pubmed-meshheading:11698641-Serine,
pubmed-meshheading:11698641-Spodoptera,
pubmed-meshheading:11698641-Transcription Factors,
pubmed-meshheading:11698641-Transcriptional Activation
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pubmed:year |
2001
|
pubmed:articleTitle |
Phosphorylation of UBF at serine 388 is required for interaction with RNA polymerase I and activation of rDNA transcription.
|
pubmed:affiliation |
Division of Molecular Biology of the Cell II, German Cancer Research Center, D-69120 Heidelberg, Germany. R.Voit@DKFZ-Heidelberg.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|