Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
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.
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.