• Register
X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

X

Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.

No
Yes

Arginine methylation of STAT1 regulates its dephosphorylation by T cell protein tyrosine phosphatase.

Transcriptional induction by interferons requires the tyrosine and serine phosphorylation of the STAT1 transcription factor as well as its amino-terminal arginine methylation. Here we show that arginine methylation of STAT1 controls the rate of STAT1 dephosphorylation by modulating its interaction with PIAS1 and the nuclear tyrosine phosphatase TcPTP. Inhibition of STAT1 arginine methylation, or mutation of STAT1 Arg-31, results in a prolonged half-life of STAT1 tyrosine phosphorylation. This effect appears to be mediated by an increased binding of PIAS1 to STAT1 in the absence of STAT1 arginine methylation and a concomitant decrease in the association of STAT1 with TcPTP. Furthermore, inhibitors of arginine methylation require the presence of PIAS1 to exert their negative regulatory effect on the dephosphorylation of STAT1.

Pubmed ID: 12171910

Authors

  • Zhu W
  • Mustelin T
  • David M

Journal

The Journal of biological chemistry

Publication Data

September 27, 2002

Associated Grants

  • Agency: NCI NIH HHS, Id: CA80105

Mesh Terms

  • Animals
  • Arginine
  • Blotting, Western
  • Cell Line
  • DNA-Binding Proteins
  • Fibroblasts
  • Humans
  • Immunoblotting
  • Interferon-alpha
  • Interferon-beta
  • Mice
  • Mutation
  • Phosphorylation
  • Precipitin Tests
  • Protein Binding
  • Protein Tyrosine Phosphatase, Non-Receptor Type 2
  • Protein Tyrosine Phosphatases
  • STAT1 Transcription Factor
  • Serine
  • T-Lymphocytes
  • Time Factors
  • Trans-Activators
  • Transcription, Genetic
  • Tyrosine