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- W32267765 abstract "Homeodomain-interacting protein kinase 2 (HIPK2) is a member of nuclear protein kinases family that act as cofactors for various transcription factors. HIPK2 was induced by UV irradiation and cisplatin treatment, implying degradation of HIPK2 in normal cells. Here we show that HIPK2 is ubiquitinated and degraded by WD40-repeat/SOCS box protein WSB-1, which process is blocked by UV irradiation. Yeast two-hybrid screen was performed to identify interacting proteins of HIPK2. Ube2d-1 and WSB-1 were characterized as HIPK2 interacting protein, which is E2 ubiquitin-conjugating enzyme and ubiquitin E3 ligase, respectively. Coexpression of WSB-1 resulted in degradation of HIPK2 via its C-terminal region. Domain analysis of WSB-1 revealed that WD40 repeats were sufficient for its interaction with and degradation of HIPK2, whereas SOCS box did not involved in degradation of HIPK2. In support of HIPK2 degradation by WSB-1, HIPK2 was polyubiquitinated by WSB-1 in vitro and in vivo. Ubiquitination of HIPK2 was observed by incubation of HIPK2 with immunoprecipitated WSB-1 complexes in vitro, but not with purified WSB-1, suggesting that WSB-1 forms a complex with other proteins to act as an E3 ubiquitin ligase. Ubiquitination and degradation of HIPK2 by WSB-1 was completely inhibited by UV irradiation and cisplatin treatment. These findings strongly illustrate regulatory mechanisms by which HIPK2 is maintained low level by WSB-1 in normal cells, and stabilized by genotoxic stresses, such as UV and cisplatin." @default.
- W32267765 created "2016-06-24" @default.
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- W32267765 date "2007-01-01" @default.
- W32267765 modified "2023-09-26" @default.
- W32267765 title "Ubiquitination and Degradation of Homeodomain‐interacting Protein Kinase 2 (HIPK2) by WSB‐1" @default.
- W32267765 doi "https://doi.org/10.1096/fasebj.21.6.a985-c" @default.
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