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Heat-shock protein 70 binds to a novel sequence in 5′ UTR of tumor suppressor SMAR1 and regulates its mRNA stability upon Prostaglandin A2 treatment
- Source :
- FEBS Letters. (6):1187-1192
- Publisher :
- Federation of European Biochemical Societies. Published by Elsevier B.V.
-
Abstract
- Here, we report Prostaglandin A2 (PGA2) induced binding of HSP70 to a novel site on φ1 SMAR1 5′ UTR which stabilizes the wild type transcript and leads to subsequent increase in SMAR1 protein levels. SMAR1 mediated cell cycle arrest is perturbed in PGA2-treated cells when HSP70 is knocked-down. Contrarily HSP70, unlike SMAR1, is overexpressed in breast cancers. We demonstrate that this is because of the inability of HSP70 to bind to the φ17 SMAR1 UTR variant which is the predominant form in breast cancers.
- Subjects :
- Untranslated region
Cell cycle checkpoint
Five prime untranslated region
Macromolecular Substances
RNA Stability
Biophysics
Prostaglandin
Breast Neoplasms
Cell Cycle Proteins
Biology
Biochemistry
Models, Biological
law.invention
chemistry.chemical_compound
Breast cancer
Structural Biology
law
Genetics
Tumor Cells, Cultured
Humans
HSP70 Heat-Shock Proteins
RNA, Messenger
mRNA stability
Molecular Biology
HSP70
Messenger RNA
Prostaglandins A
Base Sequence
Tumor Suppressor Proteins
PGA2
Wild type
Nuclear Proteins
Cell Biology
Molecular biology
Hsp70
DNA-Binding Proteins
Nucleoproteins
chemistry
Gene Expression Regulation
Suppressor
Nucleic Acid Conformation
5' Untranslated Regions
SMAR1
Protein Binding
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Issue :
- 6
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....92ec774242671bd29c06e0f86ac98e9e
- Full Text :
- https://doi.org/10.1016/j.febslet.2010.02.025