Reference : Modulation of Nod2-dependent NF-kappa B signaling by the actin cytoskeleton
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/9527
Modulation of Nod2-dependent NF-kappa B signaling by the actin cytoskeleton
English
Legrand, Sylvie mailto [Université de Liège - ULg > > GIGA-R : Virologie - Immunologie >]
Kustermans, Gaëlle mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Anatomie et cytologie pathologiques >]
Bex, Françoise [Université Libre de Bruxelles - ULB > Institute for Microbiological Research J.-M. Wiame > Laboratory of Microbiology > >]
Kufer, Thomas [Institut Pasteur and INSERM (PARIS, FRANCE) > > Unité de Pathogénie Microbienne Moléculaire > >]
Kremmer, Elisabeth [GSF-Institut für Molekulare Immunologie (Germany) > > > >]
Piette, Jacques mailto [Université de Liège - ULg > Département des sciences de la vie > GIGA-R : Virologie - Immunologie >]
1-Apr-2007
Journal of Cell Science
Company Of Biologists
120
7
1299-1310
Yes (verified by ORBi)
International
0021-9533
1477-9137
Cambridge
United Kingdom
[en] actin cytoskeleton ; NF-kappa B ; Nod2 ; Rac1
[en] Actin disruption by CytochalasinD (CytD) and LatrunculinB (LatB) induced NF-kappa B activation in myelomonocytic and intestinal epithelial cells. In an attempt to elucidate the mechanism by which actin disruption induced IKK activation, we studied the human Nod2 protein, which was able to induce NF-kappa B activation and whose expression was restricted to myelomonocytic and intestinal epithelial cells. Nod2 is thought to play key roles in pathogen defence through sensing bacteria and generating an inflammatory immune response. We showed that actin disruption by CytD significantly and specifically increased Nod2-mediated NF-kappa B signaling. Nod2 was fully partitioned in the Triton-X-100-insoluble fraction but translocated into the soluble fraction after CytD treatment, demonstrating that the presence of Nod2 in the detergent-insoluble pellet was specific to actin cytoskeleton. Confocal analysis also revealed a Nod2 colocalization with membrane-associated F-actin. Colocalization and co-immunoprecipitation assays with endogenous Rac1 have shown that Nod2 associated with activated Rac1 in membrane ruffles through both its N-terminal caspase recruitment domains (CARD) and C-terminal leucine-rich repeats (LRRs). Membrane ruffle disruption by a Rac1 dominant negative form primed Nod2-dependent NF-kappa B signaling. The recruitment of Nod2 in Rac-induced dynamic cytoskeletal structures could be a strategy to both repress the Nod2-dependent NF-kappa B signaling in unstimulated cells and rapidly mobilize Nod2 during bacterial infection.
Giga-Signal Transduction
Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS
Researchers ; Professionals ; Students
http://hdl.handle.net/2268/9527
also: http://hdl.handle.net/2268/102384
10.1242/jcs.03424

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