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Association of Ubc9, an E2 ligase for SUMO conjugation, with p53 is regulated by phosphorylation of p53
Author(s) -
Lin Jye-Yee,
Ohshima Takayuki,
Shimotohno Kunitada
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.07.059
Subject(s) - sumo protein , mdm2 , phosphorylation , ubiquitin ligase , ubiquitin , dna ligase , suppressor , chemistry , enzyme , p53 protein , ubiquitin conjugating enzyme , mutant , microbiology and biotechnology , cancer research , biology , biochemistry , apoptosis , gene
Small ubiquitin‐like modifier‐1 (SUMO‐1) conjugation to the tumor suppressor protein p53 seems to be regulated by murine double minute 2 homologue (Mdm2). It is thought that the physical association of Mdm2 with p53 is important for the enhancement of SUMO‐1 conjugation to p53. However, mutant p53 that does not associate with Mdm2 is still sumoylated, albeit at a reduced level, suggesting that sumoylation of p53 is independent of the presence of Mdm2 and there is a direct association of ubiquitin‐conjugating enzyme 9 (Ubc9), an E2 ligase for sumoylation, with p53. Here, we report evidence of the direct interaction of Ubc9 with p53. Furthermore, we observed that the interaction of Ubc9 with p53 was regulated by phosphorylation of p53. In particular, in cells treated with adriamycin that is a DNA damaging agent and that enhances phosphorylation of p53 at Ser‐20, SUMO conjugation of p53 was severely impaired possibly by reduced affinity of Ubc9 to p53.