Critical role of s465 in protein kinase C-increased rat glutamate transporter type 3 activity

Hee Jung Baik, Yueming Huang, Jacqueline M. Washington, Zhiyi Zuo

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

Glutamate transporters, also called excitatory amino acid transporters (EAATs), uptake extracellular glutamate and regulate neurotransmission. Activation of protein kinase C (PKC) increases the activity of EAAT type 3 (EAAT3), the major neuronal EAAT. We designed this study to determine which amino acid residue(s) in EAAT3 may be involved in this PKC effect. Selective potential PKC phosphorylation sites were mutated. These EAAT3 mutants were expressed in the Xenopus oocytes. Phorbol 12-myristate 13-acetate, a PKC activator, significantly increased wild-type EAAT3 activity. Mutation of serine 465 to alanine or aspartic acid, but not the mutation of threonine 5 to alanine, abolished PKC-increased EAAT3 activity. Our results suggest a critical role of serine 465 in the increased EAAT3 activity by PKC activation.

Original languageEnglish
Pages (from-to)1419-1428
Number of pages10
JournalInternational Journal of Neuroscience
Volume119
Issue number9
DOIs
StatePublished - 2009

Bibliographical note

Funding Information:
Glutamate transporters, also called excitatory amino acid transporters (EAATs), uptake extracellular glutamate and regulate neurotransmission. Activation of protein kinase C (PKC) increases the activity of EAAT type 3 (EAAT3), the major neuronal EAAT. We designed this study to determine which amino acid residue(s) in EAAT3 Received 27 April 2008. This work was carried out in the Department of Anesthesiology, University of Virginia. This study was supported by National Institutes of Health grants RO1 GM065211 and RO1 NS045983 (to Z. Zuo). Address correspondence to Dr. Zhiyi Zuo, Department of Anesthesiology, University of Virginia Health System, 1 Hospital Drive, P.O. Box 800710 Charlottesville, VA 22908-0710. E-mail: zz3c@virginia.edu

Keywords

  • Glutamate
  • Glutamate transporter
  • Protein kinase C
  • Site-directed mutagenesis

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