Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Sung KS,Go YY,Ahn JH,Kim YH,Kim Y,Choi CYdoi
10.1016/j.febslet.2005.04.053keywords:
subject
Has Abstractpub_date
2005-06-06 00:00:00pages
3001-8issue
14eissn
0014-5793issn
1873-3468pii
S0014-5793(05)00529-6journal_volume
579pub_type
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