TY - JOUR
T1 - Critical role of s465 in protein kinase C-increased rat glutamate transporter type 3 activity
AU - Baik, Hee Jung
AU - Huang, Yueming
AU - Washington, Jacqueline M.
AU - Zuo, Zhiyi
N1 - 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
PY - 2009
Y1 - 2009
N2 - 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.
AB - 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.
KW - Glutamate
KW - Glutamate transporter
KW - Protein kinase C
KW - Site-directed mutagenesis
UR - http://www.scopus.com/inward/record.url?scp=70350438418&partnerID=8YFLogxK
U2 - 10.1080/00207450903014783
DO - 10.1080/00207450903014783
M3 - Article
C2 - 19922365
AN - SCOPUS:70350438418
SN - 0020-7454
VL - 119
SP - 1419
EP - 1428
JO - International Journal of Neuroscience
JF - International Journal of Neuroscience
IS - 9
ER -