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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Binding and regulation of the transcription factor NFAT by the peptidyl prolyl cis-trans isomerase Pin1.

Nuclear factor of activated T cells (NFAT) plays a key role in T cell activation. The activation of NFAT involves calcium- and calcineurin-dependent dephosphorylation and nuclear translocation from the cytoplasm, a process that is opposed by protein kinases. We show here that the peptidyl prolyl cis-trans isomerase Pin1 interacts specifically with the phosphorylated form of NFAT. The NFAT-Pin1 interaction is mediated through the WW domain of Pin1 and the serine-proline-rich domains of NFAT. Furthermore, binding of Pin1 to NFAT inhibits the calcineurin-mediated dephosphorylation of NFAT in vitro, and overexpression of Pin1 in T cells inhibits calcium-dependent activation of NFAT in vivo. These results suggest a possible role for Pin1 in the regulation of NFAT in T cells.[1]

References

  1. Binding and regulation of the transcription factor NFAT by the peptidyl prolyl cis-trans isomerase Pin1. Liu, W., Youn, H.D., Zhou, X.Z., Lu, K.P., Liu, J.O. FEBS Lett. (2001) [Pubmed]
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