Module 4: Figure NFAT structure
The structural domains of nuclear factor of activated T cells (NFAT).
The various domains located along the length of the nuclear factor of activated T cells (NFAT) molecule perform different functions during its activation of transcription. Starting with the N-terminal region, there is an activation domain. The interaction between NFAT and calcineurin depends on two calcineurin-binding domains (A and B, shown in blue). Calcineurin then removes the 13 phosphate groups (red dots) that are clustered in four regions: a serine-rich region (SRR-1), two Ser-Pro sequences (SP-2 and SP-3) and one at a KTS site. Removal of these phosphates unveils a nuclear localization signal (NLS) that enables NFAT to enter the nucleus. Once in the nucleus, NFAT binds to DNA through the Rel-homology region (RHR), which has two parts: an N-terminal specificity domain (RYR-N), which binds to DNA, and a C-terminal dimerization domain (RHR-C), which binds to other transcription factors such as activating protein 1 (AP-1) (Module 4: Figure NFAT/AP-1/DNA complex). Modified, with permission, from Hogan, P.G., Chen, L., Nardone, J. and Rao, A. (2003) Transcriptional regulation by calcium, calcineurin, and NFAT. Genes Dev. 17:2205–2232. Copyright (2003) Cold Spring Harbor Laboratory Press; see Hogan et al. 2003.