Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
2000-6-21
pubmed:abstractText
Expression of heat shock proteins (HSPs) is controlled by heat shock transcription factors (HSFs). Vertebrates express multiple HSFs whose activities may be regulated by distinct signals. HSF3 is specifically activated in unstressed proliferating cells by direct binding to the c-myb proto-oncogene product (c-Myb), which plays an important role in cellular proliferation. This suggests that the c-Myb-induced HSF3 activation may contribute to the growth-regulated expression of HSPs. Here we report that the p53 tumor suppressor protein directly binds to HSF3 and blocks the interaction between c-Myb and HSF3. In addition, p53 stimulates the degradation of c-Myb through a proteasome-dependent mechanism, which is, at least partly, mediated by induction of Siah in certain types of cells. Induction of p53 by a genotoxic reagent in DT40 cells disrupts the HSF3-c-Myb interaction and down-regulates the expression of certain HSPs. Mutated forms of p53 found in certain tumors did not inhibit c-Myb-induced HSF3 activation. The regulation of HSF3 activity by c-Myb and p53 sheds light on the molecular events that govern HSP expression during cellular proliferation and apoptosis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Avian Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HSF3 protein, Gallus gallus, http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Luciferases, http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-myb, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Protein p53
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
275
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15578-85
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10747903-Animals, pubmed-meshheading:10747903-Avian Proteins, pubmed-meshheading:10747903-Cell Line, pubmed-meshheading:10747903-Chickens, pubmed-meshheading:10747903-Cysteine Endopeptidases, pubmed-meshheading:10747903-DNA-Binding Proteins, pubmed-meshheading:10747903-Genes, Reporter, pubmed-meshheading:10747903-Heat-Shock Proteins, pubmed-meshheading:10747903-Humans, pubmed-meshheading:10747903-Kinetics, pubmed-meshheading:10747903-Luciferases, pubmed-meshheading:10747903-Mice, pubmed-meshheading:10747903-Multienzyme Complexes, pubmed-meshheading:10747903-Mutagenesis, Site-Directed, pubmed-meshheading:10747903-Point Mutation, pubmed-meshheading:10747903-Proteasome Endopeptidase Complex, pubmed-meshheading:10747903-Proto-Oncogene Proteins c-myb, pubmed-meshheading:10747903-Recombinant Proteins, pubmed-meshheading:10747903-Trans-Activators, pubmed-meshheading:10747903-Transcription, Genetic, pubmed-meshheading:10747903-Transfection, pubmed-meshheading:10747903-Tumor Suppressor Protein p53
pubmed:year
2000
pubmed:articleTitle
p53 suppresses the c-Myb-induced activation of heat shock transcription factor 3.
pubmed:affiliation
Laboratory of Molecular Genetics, RIKEN Tsukuba Life Sciences Center, Japan Science and Technology, 3-1-1 Koyadai, Tsukuba, Ibaraki 305-0074, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't