Modulation of a recombinant glycine transporter (GLYT1b) by activation of protein kinase C

J Neurochem. 1995 Nov;65(5):1967-73. doi: 10.1046/j.1471-4159.1995.65051967.x.

Abstract

Treatment of human embryonic kidney cells (HEK 293 cells) expressing the mouse glycine transporter 1 (GLYT1b) with the protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA) decreased specific [3H]glycine uptake. This down-regulation resulted from a reduction of the maximal transport rate and was blocked by the PKC inhibitors 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine (H7) and staurosporine. The inhibitory effect of PMA treatment was also observed after removing all five predicted phosphorylation sites for PKC in GLYT1b by site-directed mutagenesis. These data indicate that glycine transport by GLYT1b is modulated by PKC activation; however, this regulation may involve indirect phosphorylation mechanisms.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Transport Systems, Neutral*
  • Carrier Proteins / metabolism*
  • Cell Line
  • Enzyme Activation
  • Glycine / metabolism
  • Glycine Plasma Membrane Transport Proteins
  • Humans
  • Membrane Potentials
  • Mutation
  • Protein Kinase C / metabolism*
  • Recombinant Proteins
  • Sodium-Hydrogen Exchangers / metabolism
  • Tetradecanoylphorbol Acetate / pharmacology

Substances

  • Amino Acid Transport Systems, Neutral
  • Carrier Proteins
  • Glycine Plasma Membrane Transport Proteins
  • Recombinant Proteins
  • SLC6A9 protein, human
  • Sodium-Hydrogen Exchangers
  • Protein Kinase C
  • Tetradecanoylphorbol Acetate
  • Glycine