Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
2004-10-18
pubmed:abstractText
The calcium-responsive transactivator (CREST) is required for the normal development of neuronal dendritic trees. Here we report that CREST is localized to sub-nuclear structures in the rat neuroendocrine pheochromocytoma PC12 cells. A yellow fluorescence protein-CREST fusion protein was expressed in HEK 293 and PC12 cells and the recombinant protein was exclusively targeted to nuclear bodies. A similar result was obtained with a Flag-tagged CREST. Deleting the N-terminal 148 or the C-terminal 79 amino acid sequences had no effect on targeting, whereas removing 164 amino acid residues from the C-terminus abolished nuclear body localization. We found that CREST did not co-localize with promyelocytic leukaemia oncoprotein (PML) body and was not targeted to PML bodies. Overexpression of CREST markedly increased the number of nuclear bodies positive for the histone acetyltransferase CREB binding protein (CBP). Double immunofluorescence staining of Flag-CREST and CBP suggested that CREST and CBP had a high degree of co-localization within the nuclear bodies. Deletion of the CBP binding domain of CREST inhibited the recruitment of CBP to CREST nuclear bodies. These results suggest that CBP recruitment to nuclear bodies by CREST may play an important role in CREST-mediated calcium-responsive transactivation, and CREST nuclear body may function as an assembly site for activators/co-activators in gene transcription control.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Alcohol Oxidoreductases, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/C-terminal binding protein, http://linkedlifedata.com/resource/pubmed/chemical/CREB-Binding Protein, http://linkedlifedata.com/resource/pubmed/chemical/CREBBP protein, human, http://linkedlifedata.com/resource/pubmed/chemical/CREST protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Calcium, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Crebbp protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/PML protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/citrate-binding transport protein, http://linkedlifedata.com/resource/pubmed/chemical/yellow fluorescent protein, Bacteria
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0304-3940
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
370
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
191-5
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:15488321-Alcohol Oxidoreductases, pubmed-meshheading:15488321-Animals, pubmed-meshheading:15488321-Bacterial Proteins, pubmed-meshheading:15488321-Blotting, Western, pubmed-meshheading:15488321-CREB-Binding Protein, pubmed-meshheading:15488321-Calcium, pubmed-meshheading:15488321-Carrier Proteins, pubmed-meshheading:15488321-Cell Count, pubmed-meshheading:15488321-Cell Line, pubmed-meshheading:15488321-Cell Nucleus, pubmed-meshheading:15488321-DNA-Binding Proteins, pubmed-meshheading:15488321-Fluorescent Antibody Technique, pubmed-meshheading:15488321-Humans, pubmed-meshheading:15488321-Luminescent Proteins, pubmed-meshheading:15488321-Mutagenesis, pubmed-meshheading:15488321-Neoplasm Proteins, pubmed-meshheading:15488321-Nuclear Proteins, pubmed-meshheading:15488321-Phosphoproteins, pubmed-meshheading:15488321-RNA, Messenger, pubmed-meshheading:15488321-Rats, pubmed-meshheading:15488321-Recombinant Proteins, pubmed-meshheading:15488321-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:15488321-Trans-Activators, pubmed-meshheading:15488321-Transcription, Genetic, pubmed-meshheading:15488321-Transcription Factors, pubmed-meshheading:15488321-Transcriptional Activation, pubmed-meshheading:15488321-Transfection, pubmed-meshheading:15488321-Tumor Suppressor Proteins
pubmed:year
2004
pubmed:articleTitle
The calcium-responsive transactivator recruits CREB binding protein to nuclear bodies.
pubmed:affiliation
Department of Pathology, University of Oklahoma Health Sciences Center, PO Box 26901, Oklahoma City, OK 73190, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't