The 'PINIT' motif, of a newly identified conserved domain of the PIAS protein family, is essential for nuclear retention of PIAS3L

被引:70
作者
Duval, D
Duval, G
Kedinger, C
Poch, O
Boeuf, H
机构
[1] ULP, INSERM, Inst Genet & Biol Mol & Cellulaire, CU Strasbourg, F-67404 Illkirch Graffenstaden, France
[2] Sanofi Synthelabo, Grp Genom Fonct, F-92500 Illkirch Graffenstaden, France
[3] Ecole Super Biotechnol Strasbourg, F-67412 Illkirch Graffenstaden, France
[4] Univ Bordeaux 2, UMR 5164, CIRID CNRS INSERM, F-33076 Bordeaux, France
关键词
embryonic stem cell; E3-type SUMO ligase; nuclear localization; PIAS; STAT repressor;
D O I
10.1016/S0014-5793(03)01116-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
PIAS proteins, cytokine-dependent STAT-associated repressors, exhibit intrinsic E3-type SUMO ligase activities and form a family of transcriptional modulators. Three conserved domains have been identified so far in this protein family, the SAP box, the MIZ-Zn finger/RING module and the acidic C-terminal domain, which are essential for protein interactions, DNA binding or SUMO ligase activity. We have identified a novel conserved domain of 180 residues in PIAS proteins and shown that its 'PINIT' motif as well as other conserved motifs (in the SAP box and in the RING domain) are independently involved in nuclear retention of PIAS3L, the long form of PIAS3, that we have characterized in mouse embryonic stem cells. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:111 / 118
页数:8
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