PMID: 9442374Jan 27, 1998Paper

Control of NF-kappa B activity by the I kappa B beta inhibitor

Immunobiology
R WeilA Israël

Abstract

The transcription factor NF-kappa B is maintained in an inactive cytoplasmic state by I kappa B inhibitors. In mammalian cells, I kappa B alpha and I kappa B beta proteins have been purified and shown to be the inhibitors of NF-kappa B through their association with the p65 or c-Rel subunits. In addition, we have isolated a third NF-kappa B inhibitor, I kappa B epsilon (1). Upon treatment with a large variety of inducers, I kappa B alpha, I kappa B beta are proteolytically degraded, resulting in NF-kappa B translocation into the nucleus. Here we show that in E29.1 T cell hybridoma I kappa B alpha and I kappa B beta are equally associated with p65 and that I kappa B beta is degraded in response to TNF alpha in contrast to what has been originally published. Our data also suggest that, unlike I kappa B alpha, I kappa B beta is constitutively phosphorylated and resynthesized as a hypophosphorylated form. The absence of slow migrating forms of I kappa B beta following stimulation suggests that the phosphorylation does not necessarily constitute the signal-induced event which targets the molecule for proteolysis.

Citations

Mar 17, 1999·Proceedings of the National Academy of Sciences of the United States of America·W J RayA M Goate
Sep 6, 2000·American Journal of Respiratory Cell and Molecular Biology·A VenkatakrishnanT S Blackwell
Mar 24, 2009·Annual Review of Immunology·Sivakumar Vallabhapurapu, Michael Karin
Mar 8, 2000·The Journal of Immunology : Official Journal of the American Association of Immunologists·M SpieckerJ K Liao
Sep 16, 2005·Proceedings of the National Academy of Sciences of the United States of America·Dong Wook KimClaude Parsot
Jul 11, 2001·Journal of Molecular and Cellular Cardiology·S B HaudekB P Giroir
May 18, 1999·The Journal of Surgical Research·A A KramerC Mendez
Jun 2, 2000·Gastroenterology·R M Schmid, G Adler

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