Topors acts as a SUMO-1 E3 ligase for p53 in vitro and in vivo.
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.
Mesh Terms:
Carrier Proteins, DNA Topoisomerases, Type I, DNA-Binding Proteins, HeLa Cells, Humans, Neoplasm Proteins, Nuclear Proteins, Protein Binding, Recombinant Fusion Proteins, SUMO-1 Protein, Transcription Factors, Tumor Suppressor Protein p53, Ubiquitin-Protein Ligases, Zinc Fingers
Carrier Proteins, DNA Topoisomerases, Type I, DNA-Binding Proteins, HeLa Cells, Humans, Neoplasm Proteins, Nuclear Proteins, Protein Binding, Recombinant Fusion Proteins, SUMO-1 Protein, Transcription Factors, Tumor Suppressor Protein p53, Ubiquitin-Protein Ligases, Zinc Fingers
FEBS Lett.
Date: Sep. 12, 2005
PubMed ID: 16122737
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