Involvement of PIAS1 in the sumoylation of tumor suppressor p53.
Sumoylation of p53 by the ubiquitin-like protein, SUMO-1/sentrin/PIC1, has been shown to stimulate its transcriptional activation activity. The SUMO E3 ligase, a key enzyme in the recognition of substrates to be sumoylated, has not yet been identified. We isolated PIAS1 (protein inhibitor of activated STAT1) as a SUMO-1 binding protein ... by yeast two-hybrid screening. In addition, PIAS1 bound p53 and Ubc9, the E2 for SUMO. PIAS1 that was mutated in the RING finger-like domain bound p53 and SUMO-1, but not Ubc9. PIAS1 catalyzed the sumoylation of p53 both in U2OS cells and in vitro in a domain-dependent manner. These data suggest that PIAS1 functions as a SUMO ligase, or possibly as a tightly bound regulator of it, toward p53.
Mesh Terms:
Amino Acid Sequence, Cell Fractionation, Cell Line, Genes, Reporter, Humans, Immunoblotting, Ligases, Molecular Sequence Data, Protein Binding, Protein Inhibitors of Activated STAT, Protein Structure, Tertiary, Proteins, Recombinant Fusion Proteins, SUMO-1 Protein, Saccharomyces cerevisiae, Sequence Alignment, Tumor Suppressor Protein p53, Two-Hybrid System Techniques, Ubiquitin-Conjugating Enzymes, Ubiquitins
Amino Acid Sequence, Cell Fractionation, Cell Line, Genes, Reporter, Humans, Immunoblotting, Ligases, Molecular Sequence Data, Protein Binding, Protein Inhibitors of Activated STAT, Protein Structure, Tertiary, Proteins, Recombinant Fusion Proteins, SUMO-1 Protein, Saccharomyces cerevisiae, Sequence Alignment, Tumor Suppressor Protein p53, Two-Hybrid System Techniques, Ubiquitin-Conjugating Enzymes, Ubiquitins
Mol. Cell
Date: Sep. 01, 2001
PubMed ID: 11583632
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