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PRMT5 C-terminal Phosphorylation Modulates a 14-3-3/PDZ Interaction Switch.

Alexsandra B Espejo1,2, Guozhen Gao1, Karynne Black1

  • 1From the Department of Epigenetics and Molecular Carcinogenesis, University of Texas M.D. Anderson Cancer Center, Smithville, Texas 78957.

The Journal of Biological Chemistry
|December 30, 2016
PubMed
Summary

Protein arginine methyltransferase 5 (PRMT5) regulation involves a novel phosphorylation-dependent switch. This switch controls interactions with PDZ and 14-3-3 proteins, crucial for cell survival.

Keywords:
14–3-3 proteinPDZ domaincell signalingprotein arginine N-methyltransferase 5 (PRMT5)protein methylationprotein phosphorylation

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Area of Science:

  • Cellular signaling
  • Protein biochemistry
  • Molecular biology

Background:

  • Protein arginine methyltransferase 5 (PRMT5) catalyzes symmetric dimethylarginine deposition in mammalian cells.
  • PRMT5 regulation is key to understanding its cellular functions.
  • A threonine phosphorylation site on PRMT5's C-terminal tail is targeted by Akt/serum- and glucocorticoid-inducible kinases.

Purpose of the Study:

  • To investigate the function of PRMT5 C-terminal tail phosphorylation.
  • To explore the prevalence of PDZ/14-3-3 interaction switching in signal transduction.
  • To identify other mammalian proteins utilizing this signaling mechanism.

Main Methods:

  • Identification of a threonine phosphorylation site on PRMT5.
  • Characterization of PRMT5 C-terminal tail interactions with PDZ and 14-3-3 proteins.
  • Development and application of a protein domain microarray harboring PDZ domains and 14-3-3 proteins.
  • Interrogation of candidate protein C-terminal tails using the microarray.

Main Results:

  • PRMT5's C-terminal tail exhibits a phosphorylation-dependent switch, binding PDZ domains when unphosphorylated and 14-3-3 proteins when phosphorylated.
  • This PDZ/14-3-3 switching is essential for PRMT5's plasma membrane association and organismal survival.
  • The signaling switch mechanism was identified in ERBB4, PGHS2, and IRK1, in addition to PRMT5 and HPV E6.

Conclusions:

  • A novel posttranslational modification-dependent interaction switch involving PDZ and 14-3-3 proteins regulates PRMT5.
  • This PDZ/14-3-3 switching mechanism appears to be a widespread biological paradigm in signal transduction.
  • Further research into this signaling mode could reveal new therapeutic targets.