New enzyme research reported from Western University, Department of Pathology
2008 FEB 5 -- New investigation results, 'NOD2 pathway activation by MDP or Mycobacterium tuberculosis infection involves the stable polyubiquitination of Rip2,' are detailed in a study published in Journal of Biological Chemistry. According to recent research published in the Journal of Biological Chemistry, "The Rip2 kinase contains a caspase recruitment domain and has been implicated in the activation of the transcriptional factor NF-kappaB downstream of Toll-like receptors, Nod-like receptors, and the T cell receptor. Although Rip2 has been linked to Nod signaling, how Nod-Rip2 proteins mediate NF-kappaB activation has remained unclear." "We find Rip2 required for Nod2-mediated NF-kappaB activation and to a lesser extent mitogen-activated protein kinase activation. We demonstrate that Rip2 and IkappaB kinase-gamma become stably polyubiquitinated upon treatment of cells with the NOD2 ligand, muramyl dipeptide. We also demonstrate a requirement for the E2-conjugating enzyme Ubc13, the E3 ubiquitin ligase Traf6, and the ubiquitin-activated kinase Tak1 in Nod2-mediated NF-kappaB activation. Rip2 polyubiquitination is also stimulated when macrophages are infected with live Mycobacterium tuberculosis but not when infected with heat-killed bacteria. Consistent with our data linking Rip2 to NOD and not Toll-like receptor signaling, M. tuberculosis-induced Rip2 polyubiquitination appears MyD88-independent," wrote Y. Yang and colleagues, Western University, Department of Pathology. The researchers concluded: "Collectively, these data reveal that the NOD2 pathway is ubiquitin-regulated and that Rip2 employs a ubiquitin-dependent mechanism to achieve NF-kappaB activation." Yang and colleagues published their study in the Journal of Biological Chemistry (NOD2 pathway activation by MDP or Mycobacterium tuberculosis infection involves the stable polyubiquitination of Rip2. Journal of Biological Chemistry, 2007;282(50):36223-9). For additional information, contact Y. Yang, Case Western University School of Medicine, Dept. of Pathology, Cleveland Ohio 44106 USA.. The publisher's contact information for the Journal of Biological Chemistry is: American Society Biochemistry Molecular Biology Inc., 9650 Rockville Pike, Bethesda, MD 20814-3996, USA. Keywords: United States, Biological Chemistry, Caspase, Cutaneous Tuberculosis, Enzyme Research, Kinase, Mycobacteria, Mycobacterium Tuberculosis, Pathology, Peptide, Proteins, Proteomics. This article was prepared by World Disease Weekly editors from staff and other reports. Copyright 2008, World Disease Weekly via NewsRx.com.
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