rdf:type |
|
lifeskim:mentions |
umls-concept:C0017337,
umls-concept:C0029419,
umls-concept:C0040624,
umls-concept:C0205369,
umls-concept:C0439851,
umls-concept:C0599894,
umls-concept:C1419771,
umls-concept:C1514562,
umls-concept:C1552596,
umls-concept:C1710082,
umls-concept:C1880177,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C1947931
|
pubmed:issue |
Pt 17
|
pubmed:dateCreated |
2001-10-8
|
pubmed:abstractText |
Key components of DNA replication and the basal transcriptional machinery as well as several tissue-specific transcription factors are compartmentalized in specialized nuclear domains. In the present study, we show that determinants of subnuclear targeting of the bone-related Runx2/Cbfa1 protein reside in the C-terminus. With a panel of C-terminal mutations, we further demonstrate that targeting of Runx2 to discrete subnuclear foci is mediated by a 38 amino acid sequence (aa 397-434). This nuclear matrix-targeting signal (NMTS) directs the heterologous Gal4 protein to nuclear-matrix-associated Runx2 foci and enhances transactivation of a luciferase gene controlled by Gal4 binding sites. Importantly, we show that targeting of Runx2 to the NM-associated foci contributes to transactivation of the osteoblast-specific osteocalcin gene in osseous cells. Taken together, these findings identify a critical component of the mechanisms mediating Runx2 targeting to subnuclear foci and provide functional linkage between subnuclear organization of Runx2 and bone-specific transcriptional control.
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pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0021-9533
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
114
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
3093-102
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:11590236-Amino Acid Sequence,
pubmed-meshheading:11590236-Animals,
pubmed-meshheading:11590236-Binding Sites,
pubmed-meshheading:11590236-Blotting, Western,
pubmed-meshheading:11590236-Cell Nucleus,
pubmed-meshheading:11590236-Core Binding Factor Alpha 1 Subunit,
pubmed-meshheading:11590236-DNA-Binding Proteins,
pubmed-meshheading:11590236-Fungal Proteins,
pubmed-meshheading:11590236-Genes, Reporter,
pubmed-meshheading:11590236-HeLa Cells,
pubmed-meshheading:11590236-Humans,
pubmed-meshheading:11590236-In Situ Hybridization,
pubmed-meshheading:11590236-Luciferases,
pubmed-meshheading:11590236-Microscopy, Fluorescence,
pubmed-meshheading:11590236-Molecular Sequence Data,
pubmed-meshheading:11590236-Mutation,
pubmed-meshheading:11590236-Neoplasm Proteins,
pubmed-meshheading:11590236-Osteocalcin,
pubmed-meshheading:11590236-Plasmids,
pubmed-meshheading:11590236-Protein Structure, Tertiary,
pubmed-meshheading:11590236-Rats,
pubmed-meshheading:11590236-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11590236-Sequence Homology, Amino Acid,
pubmed-meshheading:11590236-Signal Transduction,
pubmed-meshheading:11590236-Transcription, Genetic,
pubmed-meshheading:11590236-Transcription Factors,
pubmed-meshheading:11590236-Transcriptional Activation,
pubmed-meshheading:11590236-Tumor Cells, Cultured
|
pubmed:year |
2001
|
pubmed:articleTitle |
A specific targeting signal directs Runx2/Cbfa1 to subnuclear domains and contributes to transactivation of the osteocalcin gene.
|
pubmed:affiliation |
Department of Cell Biology and Cancer Center, University of Massachusetts Medical School, Worcester, MA 01655-0106, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|