Topors acts as a SUMO‐1 E3 ligase for p53 in vitro and in vivo
- 18 August 2005
- journal article
- Published by Wiley in FEBS Letters
- Vol. 579 (22) , 5007-5012
- https://doi.org/10.1016/j.febslet.2005.07.088
Abstract
Human Topors, which was originally identified as cellular binding partner of DNA topoisomerase I and of p53, has recently been shown to function as an ubiquitin E3 ligase for p53 in a manner dependent on its N′‐terminally located RING finger. Here, we demonstrate that Topors also enhances the conjugation of the small ubiquitin‐like modifier 1 (SUMO‐1) to p53 in vivo and in a reconstituted in vitro system. The Topors SUMO‐1 E3 ligase activity does not depend upon its RING finger motif. In HeLa cells, Topors induced p53 sumoylation was accompanied by an increase in endogenous p53 protein levels. Furthermore, Topors enhances the sumoylation of a variety of other, yet unidentified, cellular proteins.Keywords
This publication has 26 references indexed in Scilit:
- topors, a p53 and topoisomerase I-binding RING finger protein, is a coactivator of p53 in growth suppression induced by DNA damageOncogene, 2005
- Topors Functions as an E3 Ubiquitin Ligase with Specific E2 Enzymes and Ubiquitinates p53Journal of Biological Chemistry, 2004
- Protein Modification by SUMOAnnual Review of Biochemistry, 2004
- The topoisomerase I- and p53-binding protein topors is differentially expressed in normal and malignant human tissues and may function as a tumor suppressorOncogene, 2004
- SUMO: a regulator of gene expression and genome integrityOncogene, 2004
- MDM2-ARF complex regulates p53 sumoylationOncogene, 2003
- The Polycomb Protein Pc2 Is a SUMO E3Cell, 2003
- PIASy, a nuclear matrix–associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodiesGenes & Development, 2001
- Functional analysis and intracellular localization of p53 modified by SUMO-1Oncogene, 2001
- Definition of a consensus binding site for p53Nature Genetics, 1992