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10.1074/jbc.M115.661611

http://scihub22266oqcxt.onion/10.1074/jbc.M115.661611
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suck abstract from ncbi


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pmid26429911
      J+Biol+Chem 2015 ; 290 (48 ): 28675-82
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  • Poly(ADP-ribosyl)ation of FOXP3 Protein Mediated by PARP-1 Protein Regulates the Function of Regulatory T Cells #MMPMID26429911
  • Luo X ; Nie J ; Wang S ; Chen Z ; Chen W ; Li D ; Hu H ; Li B
  • J Biol Chem 2015[Nov]; 290 (48 ): 28675-82 PMID26429911 show ga
  • Poly(ADP-ribose) polymerase 1 (PARP-1) is an ADP-ribosylating enzyme participating in diverse cellular functions. The roles of PARP-1 in the immune system, however, have not been well understood. Here we find that PARP-1 interacts with FOXP3 and induces its poly(ADP-ribosyl)ation. By using PARP-1 inhibitors, we show that reduced poly(ADP-ribosyl)ation of FOXP3 results in not only FOXP3 stabilization and increased FOXP3 downstream genes but also enhanced suppressive function of regulatory T cells. Our results suggest that PARP-1 negatively regulates the suppressive function of Treg cells at the posttranslational level via FOXP3 poly(ADP-ribosyl)ation. This finding has implications for developing PARP-1 inhibitors as potential agents for the prevention and treatment of autoimmune diseases.
  • |Forkhead Transcription Factors/genetics/immunology/*metabolism [MESH]
  • |HEK293 Cells [MESH]
  • |Humans [MESH]
  • |Jurkat Cells [MESH]
  • |Poly (ADP-Ribose) Polymerase-1 [MESH]
  • |Poly Adenosine Diphosphate Ribose/genetics/immunology/*metabolism [MESH]
  • |Poly(ADP-ribose) Polymerases/genetics/immunology/*metabolism [MESH]
  • |Protein Processing, Post-Translational/*physiology [MESH]
  • |Protein Stability [MESH]


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