Section 12
Chapter 11,959

Differential interactions of the homeodomain-interacting protein kinase 2 (HIPK2) by phosphorylation-dependent sumoylation

Sung, K.S.; Go, Y.Y.; Ahn, J.-H.; Kim, Y.H.; Kim, Y.; Choi, C.Y.

Febs Letters 579(14): 3001-3008


ISSN/ISBN: 0014-5793
PMID: 15896780
DOI: 10.1016/j.febslet.2005.04.053
Accession: 011958121

Download citation:  

Homeodomain-interacting protein kinase 2 (HIPK2) interacts with and phosphorylates various transcription factors that are critical regulators of cell fate decisions and apoptosis during development. Here we show that lysine 25 of HIPK2 is the major sumoylation site, both in vitro and in vivo, and that the sumoylation of this site occurs in a phosphorylation-dependent manner. This became clear with the finding that kinase-dead HIPK2 (K221R) could not be efficiently sumoylated in vitro. The sumoylation of HIPK2 resulted in the disruption of its interaction with a Groucho corepressor. Consequently, sumoylation inhibited the regulatory activity of HIPK2 on the Groucho-mediated repression of transcription, whereas not on p53-mediated transactivation. These results suggest that phosphorylation-dependent sumoylation enables HIPK2 to drive different target gene transcription by means of differential interactions with its binding partners.

PDF emailed within 0-6 h: $19.90