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

doi:10.1080/00207450903014783

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

Department of Anesthesia and Pain Medicine

Research output: Contribution to journal › Article › peer-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 language	English
Pages (from-to)	1419-1428
Number of pages	10
Journal	International Journal of Neuroscience
Volume	119
Issue number	9
DOIs	https://doi.org/10.1080/00207450903014783
State	Published - 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: [email protected]

Keywords

Glutamate
Glutamate transporter
Protein kinase C
Site-directed mutagenesis

Access to Document

10.1080/00207450903014783

Cite this

@article{555c413d2f9244638a94e8d2c90fa20d,

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

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.",

keywords = "Glutamate, Glutamate transporter, Protein kinase C, Site-directed mutagenesis",

author = "Baik, {Hee Jung} and Yueming Huang and Washington, {Jacqueline M.} and Zhiyi Zuo",

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: [email protected]",

year = "2009",

doi = "10.1080/00207450903014783",

language = "English",

volume = "119",

pages = "1419--1428",

journal = "International Journal of Neuroscience",

issn = "0020-7454",

publisher = "Informa Healthcare",

number = "9",

}

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: [email protected]

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 -

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

Abstract

Bibliographical note

Keywords

Access to Document

Fingerprint

Cite this