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

FEBS Letters

Boeuf, H.²  Poch, O.²  Duval, G.²  Kedinger, C.¹  Duval, D.² 

[1] Ecole Supérieure de Biotechnologie de Strasbourg, P.O. Box 10413, 67412 Illkirch, France;Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, P.O. Box 10142, C.U. de Strasbourg, 67404 Illkirch Cedex, France

关键词: Embryonic stem cell;    E3-type SUMO ligase;    Nuclear localization;    PIAS;    STAT repressor;    STAT;    signal transducer and activator of transcription;    PIAS;    protein inhibitor of activated STATs;    ES;    embryonic stem;    LIF;    leukemia inhibitory factor;    SUMO;    small ubiquitin-related modifier;    SAP;    Saf-A/B;    Acinus and Pias;   

DOI  :  10.1016/S0014-5793(03)01116-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown