Duval D, Duval G, Kedinger C, Poch O, Boeuf H
Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, P.O. Box 10142, C.U. de Strasbourg, 67404 Illkirch, France.
FEBS Lett. 2003 Nov 6;554(1-2):111-8. doi: 10.1016/s0014-5793(03)01116-5.
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.
PIAS蛋白,即细胞因子依赖性STAT相关阻遏物,具有内在的E3型SUMO连接酶活性,并构成一个转录调节因子家族。到目前为止,在这个蛋白家族中已鉴定出三个保守结构域,即SAP框、MIZ锌指/RING模块和酸性C末端结构域,它们对于蛋白质相互作用、DNA结合或SUMO连接酶活性至关重要。我们在PIAS蛋白中鉴定出一个由180个残基组成的新型保守结构域,并表明其“PINIT”基序以及其他保守基序(在SAP框和RING结构域中)独立参与了PIAS3L(我们在小鼠胚胎干细胞中鉴定出的PIAS3的长形式)的核滞留。