RGD Reference Report - Modulation of cellular AP-1 DNA binding activity by heat shock proteins. - Rat Genome Database

Send us a Message
Submit Data |  Help |  Video Tutorials |  News |  Publications |  Download |  REST API |  Citing RGD |  Contact   
Search RGD Grant Resources Citing RGD About Us Contact Us
Genes Variants Community Projects QTLs Strains Markers Genome Information Ontologies Cell Lines References Download Submit Data
OntoMate (Literature Search) JBrowse (Genome Browser) Synteny Browser (VCMap) Variant Visualizer Multi-Ontology Enrichment (MOET) Gene-Ortholog Location Finder (GOLF) InterViewer (Protein-Protein Interactions) PhenoMiner (Quatitative Phenotypes) Gene Annotator OLGA (Gene List Generator) AllianceMine GViewer (Genome Viewer)
Aging & Age-Related Disease Cancer & Neoplastic Disease Cardiovascular Disease Coronavirus Disease Developmental Disease Diabetes Hematologic Disease Immune & Inflammatory Disease Infectious Disease Liver Disease Neurological Disease Obesity & Metabolic Syndrome Renal Disease Respiratory Disease Sensory Organ Disease
Find Models   new Genetic Models Autism Models Rat PhenoMiner (Quantitative Phenotypes) Chinchilla PhenoMiner Expected Ranges (Quantitative Phenotype) PhenoMiner Term Comparison Hybrid Rat Diversity Panel Phenotypes Phenotypes in Other Animal Models Animal Husbandry Strain Medical Records Phylogenetics Strain Availability Calendar Rats 101 Submissions Photo Archive
Pathways
Rat Community Forum Directory of Rat Laboratories Video Tutorials News RGD Publications RGD Presentations Archive Nomenclature Guidelines Resource Links Laboratory Resources Employment Resources

Modulation of cellular AP-1 DNA binding activity by heat shock proteins.

Authors: Carter, DA 
Citation: Carter DA FEBS Lett. 1997 Oct 13;416(1):81-5.
RGD ID: 2290538
Pubmed: PMID:9369238   (View Abstract at PubMed)

Recent studies have indicated that ubiquitously expressed molecular chaperones of the heat shock protein (Hsp) class may have an additional, nuclear, role in the regulation of gene expression. Experiments on cellular transcription factors derived from the rat adrenal gland have now shown that Hsps modulate in vitro DNA binding activity of the AP-1 factor. Both Hsc70 (p73) and Hsp70 (p72) were demonstrated to exert this effect through a mechanism that appears to be independent of both redox, and phosphorylation state. Further studies on the effect of Hsps on recombinant Fos/Jun protein binding activity indicated that the mechanism of action involves a selective attenuation of high affinity c-Fos:c-Jun binding as compared with c-Jun homodimer binding activity. Because cellular and physiological stress are associated with the induction of both AP-1 and Hsps it is apparent that Hsps may play a modulatory role in the regulation of AP-1 responsive genes.

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
identical protein binding  IPIJun (Rattus norvegicus)2290538homodimerizationRGD 
protein-containing complex binding  IPIJun (Rattus norvegicus)2290538heterodimerizationRGD 
protein-containing complex binding  IPIFos (Rattus norvegicus)2290538heterodimerizationRGD 

Objects Annotated

Genes (Rattus norvegicus)
Fos  (Fos proto-oncogene, AP-1 transcription factor subunit)
Jun  (Jun proto-oncogene, AP-1 transcription factor subunit)


Additional Information