dc.creator | Peidis, P. | en |
dc.creator | Voukkalis, N. | en |
dc.creator | Aggelidou, E. | en |
dc.creator | Georgatsou, E. | en |
dc.creator | Hadzopoulou-Cladaras, M. | en |
dc.creator | Scott, R. E. | en |
dc.creator | Nikolakaki, E. | en |
dc.creator | Giannakouros, T. | en |
dc.date.accessioned | 2015-11-23T10:45:19Z | |
dc.date.available | 2015-11-23T10:45:19Z | |
dc.date.issued | 2011 | |
dc.identifier | 10.1016/j.febslet.2010.11.054 | |
dc.identifier.issn | 0014-5793 | |
dc.identifier.uri | http://hdl.handle.net/11615/32135 | |
dc.description.abstract | A significant amount of nuclear p53 is found associated with the nuclear matrix in cells that were exposed to genotoxic stress. In this study we identified Scaffold attachment factor B1 (SAFB1), a nuclear matrix-associated protein that binds the scaffold or matrix attachment regions (S/MARs) of genomic DNA, as a novel p53-interacting protein. SAFB1 was able to associate with p53 through its C-terminal domain, while significant co-localization of the two proteins was observed in cells treated with 5-fluorouracil or mithramycin. Binding of p53 to SAFB1 had a significant functional outcome, since SAFB1 was shown to suppress p53-mediated reporter gene expression. These data suggest that nuclear matrix-associated proteins may play a critical role in regulating p53 localization and activity. Structured summary: p53 physically interacts with SRPK1a:shown by two hybrid (view interaction) p53 physically interacts with SRPK1a:shown by pull down (view interaction) p53 physically interacts with SRPK1a:shown by anti bait coimmunoprecipitation (view interaction) p53 physically interacts with SRPK1a:shown by anti tag coimmunoprecipitation (view interaction) SAFB1 physically interacts with p53:shown by pull down (view interactions 1, 2) SAFB1 physically interacts with p53:shown by anti bait coimmunoprecipitation (view interactions 1, 2) SAFB1 and p53 colocalize:shown by fluorescence microscopy (view interaction) SAFB2 physically interacts with p53:shown by pull down (view interaction) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved. | en |
dc.source | Febs Letters | en |
dc.source.uri | <Go to ISI>://WOS:000285921500013 | |
dc.subject | Scaffold Attachment Factor B1 | en |
dc.subject | p53 | en |
dc.subject | SRPK1a | en |
dc.subject | Nuclear matrix | en |
dc.subject | Transcription regulation | en |
dc.subject | ATTACHMENT FACTOR-B | en |
dc.subject | GENE-EXPRESSION | en |
dc.subject | NUCLEAR EXPORT | en |
dc.subject | MUTANT P53 | en |
dc.subject | PROTEIN | en |
dc.subject | DNA | en |
dc.subject | BINDING | en |
dc.subject | CELLS | en |
dc.subject | MATRIX | en |
dc.subject | RNA | en |
dc.subject | Biochemistry & Molecular Biology | en |
dc.subject | Biophysics | en |
dc.subject | Cell Biology | en |
dc.title | SAFB1 interacts with and suppresses the transcriptional activity of p53 | en |
dc.type | journalArticle | en |