Reference : The inositol phosphatase SHIP-1 inhibits NOD2-induced NF-κB activation by disturbing the...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/125601
The inositol phosphatase SHIP-1 inhibits NOD2-induced NF-κB activation by disturbing the interaction of XIAP with RIP2
English
Condé, Claude [Université de Liège - ULg > > GIGA-R : Virologie - Immunologie >]
Rambout, Xavier [Université de Liège - ULg > Chimie et bio-industries > Biologie cell. et moléc. >]
Lebrun, Marielle [Université de Liège - ULg > Département des sciences de la vie > GIGA-R : Virologie et immunologie >]
Lecat, Aurore mailto [Université de Liège - ULg > > GIGA-R : Virologie - Immunologie >]
Di Valentin, Emmanuel mailto [Université de Liège - ULg > Département des sciences de la vie > GIGA-R : Virologie et immunologie >]
Dequiedt, Franck mailto [Université de Liège - ULg > > GIGA-Research >]
Piette, Jacques mailto [Université de Liège - ULg > Département des sciences de la vie > GIGA-R : Virologie - Immunologie >]
Gloire, Geoffrey mailto [Université de Liège - ULg > > Interface Entreprises-Université >]
Legrand, Sylvie mailto [Université de Liège - ULg > > GIGA-R : Virologie - Immunologie >]
2012
PLoS ONE
Public Library of Science
Yes (verified by ORBi)
International
1932-6203
San Franscisco
CA
[en] SHIP-1 is an inositol phosphatase predominantly expressed in hematopoietic cells. Over the ten past years, SHIP-1 has been described as an important regulator of immune functions. Here, we characterize a new inhibitory function for SHIP-1 in NOD2 signaling. NOD2 is a crucial cytoplasmic bacterial sensor that activates proinflammatory and antimicrobial responses upon bacterial invasion. We observed that SHIP-1 decreases NOD2-induced NF-κB activation in macrophages. This negative regulation relies on its interaction with XIAP. Indeed, we observed that XIAP is an essential mediator of the NOD2 signaling pathway that enables proper NF-κB activation in macrophages. Upon NOD2 activation, SHIP-1 C-terminal proline rich domain (PRD) interacts with XIAP, thereby disturbing the interaction between XIAP and RIP2 in order to decrease NF-κB signaling.
http://hdl.handle.net/2268/125601

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