共 50 条
SUMO modification negatively modulates the transcriptional activity of CREB-binding protein via the recruitment of Daxx
被引:96
|作者:
Kuo, HY
Chang, CC
Jeng, JC
Hu, HM
Lin, DY
Maul, GG
Kwok, RPS
Shih, HM
[1
]
机构:
[1] Acad Sinica, Grad Inst Life Sci, Natl Def Med Ctr, Taipei 11529, Taiwan
[2] Acad Sinica, Inst Biomed Sci, Taipei 11529, Taiwan
[3] Natl Hlth Res Inst, Div Mol & Genom Med, Taipei 11529, Taiwan
[4] Wistar Inst Anat & Biol, Philadelphia, PA 19104 USA
[5] Univ Michigan, Dept Obstet & Gynecol & Biol Chem, Ann Arbor, MI 48109 USA
来源:
关键词:
protein-protein interaction;
posttranslational modification;
transcriptional repression;
SENP2;
histone deacetylase 2;
D O I:
10.1073/pnas.0504460102
中图分类号:
O [数理科学和化学];
P [天文学、地球科学];
Q [生物科学];
N [自然科学总论];
学科分类号:
07 ;
0710 ;
09 ;
摘要:
Small ubiquitin-like modifier (SUMO) modification is emerging as an important control in transcription regulation. Here, we show that CREB-binding protein (CBP), a versatile transcriptional coactivator for numerous transcription factors in response to diverse signaling events, can be modified by SUMO-1 at lysine residues 999, 1034, and 1057 both in vitro and in vivo. Mutation of the SUMO acceptor lysine residues either individually or in combination enhanced CBP transcriptional activity, and expression of a SUMO protease SENP2 potentiated the transcriptional activity of CBP wild-type but not its sumoylation mutant, indicating that SUMO modification negatively regulates CBP transcriptional activity. Furthermore, we demonstrated an interaction of SUMO-1-modified CBP with the transcriptional corepressor Daxx and an essential role of Daxx in mediating SUMO-dependent transcriptional regulation of CBP through histone deacetylase 2 recruitment. Together, our findings indicate that SUMO modification and subsequent recruitment of Daxx represent a previously undescribed mechanism in modulating CBP transcriptional potential.
引用
收藏
页码:16973 / 16978
页数:6
相关论文