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 journalArticleResearchpeer-review

39 Citations (Scopus)

Abstract

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
Pages (from-to)105-108
Number of pages4
JournalFEBS Letters
Volume496
Issue number2-3
DOIs
StatePublished - 11 May 2001

Fingerprint

Peptidylprolyl Isomerase
NFATC Transcription Factors
Transcription Factors
T-cells
Calcineurin
Chemical activation
T-Lymphocytes
Calcium
NIMA-Interacting Peptidylprolyl Isomerase
Proline
Cell Communication
Protein Kinases
Serine
Cytoplasm

Keywords

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

Cite this

Liu, Weifeng ; Youn, Hong-Duk ; Zhou, Xiao Zhen ; Lu, Kun Ping ; Liu, Jun O. / Binding and regulation of the transcription factor NFAT by the peptidyl prolyl cis-trans isomerase Pin1. In: FEBS Letters. 2001 ; Vol. 496, No. 2-3. pp. 105-108.
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abstract = "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.",
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Binding and regulation of the transcription factor NFAT by the peptidyl prolyl cis-trans isomerase Pin1. / Liu, Weifeng; Youn, Hong-Duk; Zhou, Xiao Zhen; Lu, Kun Ping; Liu, Jun O.

In: FEBS Letters, Vol. 496, No. 2-3, 11.05.2001, p. 105-108.

Research output: Contribution to journalArticleResearchpeer-review

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AU - Liu, Weifeng

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AB - 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.

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