http://precedings.nature.com/tags/phosphorylation Recently posted documents tagged with 'phosphorylation' Nature Publishing Group en Nature Precedings http://precedings.nature.com/images/header_logo.gif http://precedings.nature.com http://dx.doi.org/10.1038/npre.2008.2273.1 Our comparative analysis of eukaryotic cell-cycle complexes reveals that the identity of the periodically expressed subunits differs significantly between organisms and is often mirrored by changes in cell-cycle-dependent phosphorylation of the protein products. This indicates that many different solutions have evolved for just-in-time assembly of the same molecular machines. http://dx.doi.org/10.1038/npre.2008.2273.1 Tue, 09 Sep 2008 11:49:12 UTC Just-in-time assembly of cell-cycle protein complexes doi:10.1038/npre.2008.2273.1 2008-09-09 Lars J. Jensen Nature Precedings 2008-09-09T11:49:12Z Poster Molecular Cell Biology Bioinformatics http://creativecommons.org/licenses/by/3.0/ http://precedings.nature.com/documents/2107/version/1 The nuclear retinoic acid (RA) receptor alpha (RARα) is a transcriptional transregulator that controls the expression of specific gene subsets through binding at response elements and dynamic interactions with coregulators, which are coordinated by the ligand. Here, we highlighted a novel paradigm in which the transcription of RARα-target genes is controlled by phosphorylation cascades initiated by the rapid RA activation of the p38MAPK/MSK1 pathway. We demonstrate that MSK1 phosphorylates RARα at S369 located in the Ligand Binding Domain, allowing the binding of TFIIH and thereby phosphorylation of the N-terminal domain at S77 by cdk7/cyclin H. MSK1 also phosphorylates Histone H3 at S10. Finally, the phosphorylation cascade initiated by MSK1 is required for the recruitment of RARα/TFIIH complexes to response elements and subsequently for RARα target genes activation. Cancer cells characterized by a deregulated p38MAPK/MSK1 pathway, do not respond to RA, outlining the essential contribution of the RA-triggered phosphorylation cascade in RA signaling. http://precedings.nature.com/documents/2107/version/1 Wed, 23 Jul 2008 09:46:07 UTC A coordinated phosphorylation cascade initiated by MSK1 directs RAR alpha recruitment to target gene promoters hdl:10101/npre.2008.2107.1 2008-07-23 Cecile Rochette-Egly Nature Precedings 2008-07-23T09:46:07Z Manuscript Molecular Cell Biology http://creativecommons.org/licenses/by/3.0/ http://precedings.nature.com/documents/2079/version/1 We define phosphovariants as genetic variations that change phosphorylation sites or their interacting kinases. Considering the essential role of phosphorylation in protein functions, it is highly likely that phosphovariants change protein functions and may constitute a proportion of the mechanisms by which genetic variations cause individual differences or diseases. We categorized phosphovariants into three subtypes and developed a system that predicts them. Our method can be used to screen important polymorphisms and help to identify the mechanisms of genetic diseases. http://precedings.nature.com/documents/2079/version/1 Mon, 14 Jul 2008 20:29:00 UTC Genome-wide analysis to predict protein sequence variations that change phosphorylation sites or their corresponding kinases hdl:10101/npre.2008.2079.1 2008-07-14 Jong Hun Kim Nature Precedings 2008-07-14T20:29:00Z Manuscript Genetics & Genomics Bioinformatics http://creativecommons.org/licenses/by/3.0/