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Arginine methylation of NIP45 modulates cytokine gene expression in effector T lymphocytes

Academic Article
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Overview

authors

  • Mowen, Kerri
  • Schurter, B. T.
  • Fathman, J. W.
  • David, M.
  • Glimcher, L. H.

publication date

  • August 2004

journal

  • Molecular Cell  Journal

abstract

  • Posttranslational modification of proteins within T cell receptor signaling cascades allows T lymphocytes to rapidly initiate an appropriate immune response. Here we report a role for arginine methylation in regulating cytokine gene transcription in the T helper lymphocyte. Inhibition of arginine methylation impaired the expression of several cytokine genes, including the signature type 1 and type 2 helper cytokines, interferon gamma, and interleukin-4. T cell receptor signaling increased expression of the protein arginine methyltransferase PRMT1, which in turn methylated the nuclear factor of activated T cells (NFAT) cofactor protein, NIP45. Arginine methylation of the amino terminus of NIP45 modulated its interaction with NFAT and resulted in augmented cytokine production, while T cells from mice lacking NIP45 had impaired expression of IFNgamma and IL-4. Covalent modification of NIP45 by arginine methylation is an important mechanism of regulating the expression of NFAT-dependent cytokine genes.

subject areas

  • Amino Acid Sequence
  • Animals
  • Arginine
  • Carrier Proteins
  • Cells, Cultured
  • Cytokines
  • DNA-Binding Proteins
  • Gene Expression Regulation
  • Humans
  • Interferon-gamma
  • Interleukin-4
  • Intracellular Signaling Peptides and Proteins
  • Methylation
  • Mice
  • Mice, Inbred BALB C
  • Molecular Sequence Data
  • NFATC Transcription Factors
  • Nuclear Proteins
  • Protein-Arginine N-Methyltransferases
  • Receptors, Antigen, T-Cell
  • Recombinant Fusion Proteins
  • Signal Transduction
  • T-Lymphocytes, Helper-Inducer
  • Transcription Factors
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Identity

International Standard Serial Number (ISSN)

  • 1097-2765

Digital Object Identifier (DOI)

  • 10.1016/j.molcel.2004.06.042

PubMed ID

  • 15327772
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Additional Document Info

start page

  • 559

end page

  • 571

volume

  • 15

issue

  • 4

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