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| Biochem. Biophys. Res. Commun. Mar (2003); 302(2):421-6 | |
| HMGB1 interacts differentially with members of the Rel family of transcription factors. | |
| Agresti A, Lupo R, Bianchi ME, Muller S | |
| DIBIT, San Raffaele Scientific Institute, Milan, Italy. | |
| Abstract: HMGB1 is an architectural factor that enhances the DNA binding affinity of several proteins. We have investigated the influence of HMGB1 on DNA binding by members of the Rel family. HMGB1 enhances DNA binding by p65/p50 and p50/p50, but reduces binding by p65/p65, c-Rel/c-Rel, p65/c-Rel, and p50/c-Rel. In pull-down assays, HMGB1 interacts directly with the p50 subunit via its HMG boxes and this interaction is weakened by the presence of the acidic tail. Functionally, HMGB1 is required for the NF-kappaB-dependent expression of the adhesion molecule VCAM-1. | |
| [PUBMED: 12604365] |   |
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| BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9. |