Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10873319 | FEBS Letters | 2005 | 6 Pages |
Abstract
The transcription factor NFAT1 is activated through dephosphorylation of multiple serine residues, contained within the SRR1 and SP motifs. The phosphorylation status of these motifs regulates the subcellular localisation of NFAT1 via a conformational switch. Here, we discuss two molecular mechanisms for NFAT1 activation that resemble network-oriented approaches. In the modular mechanism, import and export are regulated separately by the SRR1 and SP motifs, respectively, whereas in the concerted model all residues jointly control both processes. Using simulations of a computational model, we show that both mechanisms may be compatible with recent experimental data on the import and export kinetics of NFAT1.
Keywords
serine-rich regionnESCKILMBNFATNLSLiClGSK3nuclear magnetic resonanceFluorescence resonance energy transferFRETCSANMRConformational switchcyclosporin Anuclear export signalnuclear localisation signalnuclear factor of activated T-cellsPhosphorylationLeptomycin Blithium chlorideMathematical modelModularitymitogen-activated protein kinasecasein kinase IMAP kinaseglycogen synthase kinase-3
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Authors
Carlos Salazar, Thomas Höfer,