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

D. Duval (1, 2) , G. Duval (2) , C. Kedinger (3) , Olivier Poch (2) , H. Boeuf (2, 4)

1 Sanofi-Synthelabo
2 IGBMC - Institut de génétique et biologie moléculaire et cellulaire
3 ESBS - Ecole Supérieure de Biotechnologie de Strasbourg
4 CIRID - Composantes innées de la réponse immunitaire et différenciation

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.

Domaines: Biochimie, Biologie Moléculaire

D. Duval, G. Duval, C. Kedinger, Olivier Poch, H. Boeuf. The 'PINIT' motif, of a newly identified conserved domain of the PIAS protein family, is essential for nuclear retention of PIAS3L. FEBS Letters, 2003, 554 (1-2), pp.111-118. ⟨10.1016/s0014-5793(03)01116-5⟩. ⟨hal-04145145⟩