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P53 regulation

3 out of 4 ain't bad

Nature Reviews Cancer volume 2, page 5 (2002)Cite this article

Thomas G. Hofmann et al. had previously cloned human HIPK2, but Gabriella D'Orazi et al. isolated HIPK2 in a yeast two-hybrid screen, using a p53 mutant that lacked the transactivation domain as the bait. This provided the first insight into its function.

The HIPK2–p53 interaction was confirmed in vitro and in vivo. Hofmann et al. showed it to be independent of HIPK2's kinase activity; a point mutation (K221A) renders the kinase inactive, yet it can still bind p53. HIPK2 and p53 also co-localize in nuclear structures known as nuclear bodies, which is facilitated by PML3 (see picture). CREB-binding protein (CBP), which acetylates and activates p53, also localizes in nuclear bodies, indicating that they could be structures in which p53 is modified.

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ORIGINAL RESEARCH PAPERS

  1. Hofmann, T. G. et al. Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2. Nature Cell Biol. 4, 1–12 (2002)

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  2. D'Orazi, G. et al. Homeodomain-interacting protein kinase-2 phosphorylates p53 at Ser 46 and mediates apoptosis. Nature Cell Biol. 4, 13–19 (2002) | Article |

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Authors
  1. Emma Greenwood
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Greenwood, E. 3 out of 4 ain't bad. Nat Rev Cancer 2, 5 (2002). https://doi.org/10.1038/nrc715

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  • DOI: https://doi.org/10.1038/nrc715

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