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Activation of the transcription factor NFAT1: concerted or modular regulation?
Author(s) -
Salazar Carlos,
Höfer Thomas
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.12.029
Subject(s) - transcription factor , serine , dephosphorylation , phosphorylation , modular design , chemistry , computational biology , subcellular localization , microbiology and biotechnology , biology , biophysics , biochemistry , computer science , gene , phosphatase , operating system
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.