The Inositol Phosphatase SHIP-1 Inhibits NOD2-Induced NF-κB Activation by Disturbing the Interaction of XIAP with RIP2

被引：29

作者：

Conde, Claude ^{[1
]}

Rambout, Xavier ^{[2
]}

Lebrun, Marielle ^{[1
]}

Lecat, Aurore ^{[1
]}

Di Valentin, Emmanuel ^{[3
]}

Dequiedt, Franck ^{[2
]}

Piette, Jacques ^{[1
]}

Gloire, Geoffrey ^{[4
]}

Legrand, Sylvie ^{[1
]}

机构：

[1] Univ Liege, Lab Virol & Immunol, Signal Transduct Unit, GIGA R, Liege, Belgium

[2] Univ Liege, Signal Transduct Unit, GIGA R, Lab Prot Signaling & Interact, Liege, Belgium

[3] Univ Liege, GIGA Viral Vector Platform, GIGA R, Liege, Belgium

[4] Interface Entreprises Univ Liege Sci Pk, Liege, Belgium

来源：

PLOS ONE | 2012年 / 7卷 / 07期

关键词：

X-LINKED INHIBITOR; FC-GAMMA-RIIB; CROHNS-DISEASE; SIGNAL-TRANSDUCTION; BINDING DOMAIN; PROTEIN; NOD2; RECEPTOR; APOPTOSIS; INNATE;

D O I：

10.1371/journal.pone.0041005

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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-kappa B 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-kappa B 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-kappa B signaling.

引用

页数：14

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