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

• Published in: FEBS letters 2003-11, Vol.554 (1-2), p.111-118
• Main Authors: Duval, D., Duval, G., Kedinger, C., Poch, O., Boeuf, H.
• Format: Article
• Language: English
• Subjects: Active Transport, Cell Nucleus; Amino Acid Motifs; Amino Acid Sequence; Animals; Biochemistry, Molecular Biology; Carrier Proteins - chemistry; Carrier Proteins - genetics; Carrier Proteins - metabolism; Cell Line; Cloning, Molecular; Conserved Sequence; DNA, Complementary; E3-type SUMO ligase; Embryonic stem cell; ES, embryonic stem; Gene Expression Regulation; Genetic Variation; Intracellular Signaling Peptides and Proteins; LIF, leukemia inhibitory factor; Life Sciences; Mice; Molecular Sequence Data; Nuclear localization; PIAS; PIAS, protein inhibitor of activated STATs; Protein Inhibitors of Activated STAT; Protein Structure, Tertiary; SAP, Saf-A/B, Acinus and Pias; Sequence Alignment; STAT repressor; STAT, signal transducer and activator of transcription; SUMO, small ubiquitin-related modifier
• ISSN: 0014-5793; 1873-3468
• 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.