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

Weifeng Liu, Hong Duk Youn, Xiao Zhen Zhou, Kun Ping Lu, Jun O. Liu

Research output: Contribution to journalArticle


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.

Original languageEnglish (US)
Pages (from-to)105-108
Number of pages4
JournalFEBS Letters
Issue number2-3
StatePublished - May 11 2001



  • Calcineurin
  • Calcium signaling
  • Nuclear factor of activated T cells
  • Pin1
  • Ser-Pro repeat
  • WW domain

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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