Tollip is a mediator of protein sumoylation. (Articolo in rivista)

Type
Label
  • Tollip is a mediator of protein sumoylation. (Articolo in rivista) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Alternative label
  • Ciarrocchi A, D'Angelo R, Cordiglieri C, Rispoli A, Santi S, Riccio M, Carone S, Mancia AL, Paci S, Cipollini E, Ambrosetti D, Melli M. (2009)
    Tollip is a mediator of protein sumoylation.
    in PloS one
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Ciarrocchi A, D'Angelo R, Cordiglieri C, Rispoli A, Santi S, Riccio M, Carone S, Mancia AL, Paci S, Cipollini E, Ambrosetti D, Melli M. (literal)
Pagina inizio
  • e4404 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 4 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Biology, Bologna University, Bologna, Italy, Institute of Organ Transplantation and Immunocitology-ITOI, C.N.R, Bologna, Italy (literal)
Titolo
  • Tollip is a mediator of protein sumoylation. (literal)
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. (literal)
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