Activation of the transcription factor NFAT1: concerted or modular regulation?
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.
Salazar
Carlos
C
Theoretische Biophysik, Institut für Biologie, Humboldt-Universität zu Berlin, Invalidenstrasse 42, 10115 Berlin, Germany. carlos.salazar@rz.hu-berlin.de
Höfer
Thomas
T
D004268:DNA-Binding Proteins / Q000378:metabolism*; D007700:Kinetics; D050778:NFATC Transcription Factors; D009687:Nuclear Proteins / Q000378:metabolism*; D010766:Phosphorylation; D021381:Protein Transport; D013347:Subcellular Fractions / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism*
D004268:DNA-Binding Proteins; D050778:NFATC Transcription Factors; D009687:Nuclear Proteins; D014157:Transcription Factors