Riboflavin kinase couples TNF receptor 1 to NADPH oxidase

Benjamin Yazdanpanah, Katja Wiegmann, Vladimir Tchikov, Oleg Krut, Carola Pongratz, Michael Schramm, Andre Kleinridders, Thomas Wunderlich, Hamid Kashkar, Olaf Utermöhlen, Jens C. Brüning, Stefan Schütze and Martin Krönke ()
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Benjamin Yazdanpanah: Institute for Medical Microbiology, Immunology and Hygiene,
Katja Wiegmann: Institute for Medical Microbiology, Immunology and Hygiene,
Vladimir Tchikov: Institute for Immunology, University of Kiel
Oleg Krut: Institute for Medical Microbiology, Immunology and Hygiene,
Carola Pongratz: Institute for Medical Microbiology, Immunology and Hygiene,
Michael Schramm: Institute for Medical Microbiology, Immunology and Hygiene,
Andre Kleinridders: Institute for Genetics, University of Cologne, 50935 Cologne, Germany
Thomas Wunderlich: Institute for Genetics, University of Cologne, 50935 Cologne, Germany
Hamid Kashkar: Institute for Medical Microbiology, Immunology and Hygiene,
Olaf Utermöhlen: Institute for Medical Microbiology, Immunology and Hygiene,
Jens C. Brüning: Center of Molecular Medicine Cologne,
Stefan Schütze: Institute for Immunology, University of Kiel
Martin Krönke: Institute for Medical Microbiology, Immunology and Hygiene,

Nature, 2009, vol. 460, issue 7259, 1159-1163

Abstract: Riboflavin kinase: linking TNF receptor to NAPDH oxidation Riboflavin kinase has been identified as a novel interacting partner for the death domain of receptor-1 for tumour necrosis factor (TNF-R1). It is required to recruit to and functionally couple p22phox to TNF-R1. As p22phox is the catalytic subunit of NADPH oxidases Nox1–4, this has general implications for TNF-induced NADPH oxidase activation and reactive oxygen species (ROS) production by many cell types and tissues. These findings may also be of relevance to the role of ROS in host defence and in the pathogenesis of many diseases including inflammation or atherosclerosis.

Date: 2009
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DOI: 10.1038/nature08206

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