دورية أكاديمية

Tollip is a mediator of protein sumoylation.

التفاصيل البيبلوغرافية
العنوان: Tollip is a mediator of protein sumoylation.
المؤلفون: Alessia Ciarrocchi, Romina D'Angelo, Chiara Cordiglieri, Ada Rispoli, Spartaco Santi, Massimo Riccio, Simona Carone, Anna Laura Mancia, Simone Paci, Elena Cipollini, Davide Ambrosetti, Marialuisa Melli
المصدر: PLoS ONE, Vol 4, Iss 2, p e4404 (2009)
بيانات النشر: Public Library of Science (PLoS), 2009.
سنة النشر: 2009
المجموعة: LCC:Medicine
LCC:Science
مصطلحات موضوعية: Medicine, Science
الوصف: 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.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1932-6203
العلاقة: http://europepmc.org/articles/PMC2635935?pdf=renderTest; https://doaj.org/toc/1932-6203Test
DOI: 10.1371/journal.pone.0004404
الوصول الحر: https://doaj.org/article/8c3dd75eba6d445a839de36b4df9ddbeTest
رقم الانضمام: edsdoj.8c3dd75eba6d445a839de36b4df9ddbe
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:19326203
DOI:10.1371/journal.pone.0004404