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

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 Lett

journal_title

FEBS letters

authors

Sung KS,Go YY,Ahn JH,Kim YH,Kim Y,Choi CY

doi

10.1016/j.febslet.2005.04.053

keywords:

subject

Has Abstract

pub_date

2005-06-06 00:00:00

pages

3001-8

issue

14

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(05)00529-6

journal_volume

579

pub_type

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