tailieunhanh - Báo cáo khoa học: Phosphorylation of NF-jB proteins by cyclic GMP-dependent kinase A noncanonical pathway to NF-jB activation

The transcription factorNF-jB is activated in cellular stress responses. This requires rapid regulation of its function, which is accomplished, in part, by various modes of phos-phorylation. Even though diverseDNAbinding subunits of NF-jB proteins may transactivate fromdistinct recognition sequences, the differential regulation of transcription from the large number of NF-jB responsive sites in various gene promoters andenhancershasbeen incompletelyunderstood. | Eur. J. Biochem. 270 2174-2185 2003 FEBS 2003 doi Phosphorylation of NF-kB proteins by cyclic GMP-dependent kinase A noncanonical pathway to NF-kB activation Bin He1 and Georg F. Weber1 2 1 Department of Radiation Oncology New England Medical Center Boston MA USA 2Immunology Program Sackler School of Graduate Biomedical Research Tufts University Medical School Boston MA USA The transcription factor NF-kB is activated in cellular stress responses. This requires rapid regulation of its function which is accomplished in part by various modes of phosphorylation. Even though diverse DNA binding subunits of NF-kB proteins may transactivate from distinct recognition sequences the differential regulation of transcription from the large number of NF-kB responsive sites in various gene promoters and enhancers has been incompletely understood. The cyclic GMP-dependent kinase PKG is an important mediator of signal transduction that may induce gene expression through cAMP response element binding protein CREB and through other yet undefined mechanisms. We have previously characterized a signal transduction pathway that leads to activation-induced cell death in T-lymphocytes and involves the activation of PKG. Here we demonstrate that the NF-kB proteins p65 p49 also called p52 and p50 are specific substrates for this kinase. PKG dose-dependently increases the transactivating activity of p65 from the NF-kB consensus sequence. It also mediates dose-dependently an increase in transcriptional activity by p49 or p50 from a unique CCAAT enhance binding protein C EBP -associ-ated NF-kB site but not from the consensus site. Phosphorylation of p65 p50 or p49 does not alter their subcellular distribution. Because the release of cytosolic p65 p50 heterodimers into the nucleus is by itself insufficient to differentiate all the numerous NF-kB promoter sequences phosphorylation of the DNA-binding subunits reveals a form of differential regulation of NF-kB .

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