Tollip is an interactor of the interleukin-1 receptor involved in its activation. The endosomal turnover of ubiquitylated IL-1RI is also controlled by Tollip. Furthermore, together with Tom1, Tollip has a general role in endosomal protein traffic. This work shows that Tollip is involved in the sumoylation process. Using the yeast two-hybrid technique, we have isolated new Tollip partners including two sumoylation enzymes, SUMO-1 and the transcriptional repressor Daxx. The interactions were confirmed by GST-pull down experiments and immunoprecipitation of the co-expressed recombinants. More specifically, we show that the TIR domain of the cytoplasmic region of IL-1RI is a sumoylation target of Tollip. The sumoylated and unsumoylated RanGAP-1 protein also interacts with Tollip, suggesting a possible role in RanGAP-1 modification and nuclear-cytoplasmic protein translocation. In fact, Tollip is found in the nuclear bodies of SAOS-2/IL-1RI cells where it colocalizes with SUMO-1 and the Daxx repressor. We conclude that Tollip is involved in the control of both nuclear and cytoplasmic protein traffic, through two different and often contrasting processes: ubiquitylation and sumoylation.

Tollip is a mediator of protein sumoylation / Alessia, Ciarrocchi; Romina, D'Angelo; Chiara, Cordiglieri; Ada, Rispoli; Spartaco, Santi; Riccio, Massimo; Simona, Carone; Anna Laura, Mancia; Simone, Paci; Elena, Cipollini; Davide, Ambrosetti; Marialuisa, Melli. - In: PLOS ONE. - ISSN 1932-6203. - ELETTRONICO. - 4:2(2009), pp. 1-10. [10.1371/journal.pone.0004404]

Tollip is a mediator of protein sumoylation

RICCIO, Massimo;
2009

Abstract

Tollip is an interactor of the interleukin-1 receptor involved in its activation. The endosomal turnover of ubiquitylated IL-1RI is also controlled by Tollip. Furthermore, together with Tom1, Tollip has a general role in endosomal protein traffic. This work shows that Tollip is involved in the sumoylation process. Using the yeast two-hybrid technique, we have isolated new Tollip partners including two sumoylation enzymes, SUMO-1 and the transcriptional repressor Daxx. The interactions were confirmed by GST-pull down experiments and immunoprecipitation of the co-expressed recombinants. More specifically, we show that the TIR domain of the cytoplasmic region of IL-1RI is a sumoylation target of Tollip. The sumoylated and unsumoylated RanGAP-1 protein also interacts with Tollip, suggesting a possible role in RanGAP-1 modification and nuclear-cytoplasmic protein translocation. In fact, Tollip is found in the nuclear bodies of SAOS-2/IL-1RI cells where it colocalizes with SUMO-1 and the Daxx repressor. We conclude that Tollip is involved in the control of both nuclear and cytoplasmic protein traffic, through two different and often contrasting processes: ubiquitylation and sumoylation.
2009
4
2
1
10
Tollip is a mediator of protein sumoylation / Alessia, Ciarrocchi; Romina, D'Angelo; Chiara, Cordiglieri; Ada, Rispoli; Spartaco, Santi; Riccio, Massimo; Simona, Carone; Anna Laura, Mancia; Simone, Paci; Elena, Cipollini; Davide, Ambrosetti; Marialuisa, Melli. - In: PLOS ONE. - ISSN 1932-6203. - ELETTRONICO. - 4:2(2009), pp. 1-10. [10.1371/journal.pone.0004404]
Alessia, Ciarrocchi; Romina, D'Angelo; Chiara, Cordiglieri; Ada, Rispoli; Spartaco, Santi; Riccio, Massimo; Simona, Carone; Anna Laura, Mancia; Simone, Paci; Elena, Cipollini; Davide, Ambrosetti; Marialuisa, Melli
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11380/596017
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