Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit

Katherine W. Roche, Richard J. O'Brien, Andrew L. Mammen, Jeffrey Bernhardt, Richard L Huganir

Research output: Contribution to journalArticle

Abstract

We have characterized the phosphorylation of the glutamate receptor subunit GluR1, using biochemical and electrophysiological techniques. GluR1 is phosphorylated on multiple sites that are all located on the C-terminus of the protein. Cyclic AMP-dependent protein kinase specifically phosphorylates SER-845 of GluR1 in transfected HEK cells and in neurons in culture. Phosphorylation of this residue results in a 40% potentiation of the peak current through GluR1 homomeric channels. In addition, protein kinase C specifically phosphorylates Ser-831 of GluR1 in HEK-293 cells and in cultured neurons. These results are consistent with the recently proposed transmembrane topology models of glutamate receptors, in which the C-terminus is intracellular. In addition, the modulation of GluR1 by PKA phosphorylation of Ser-845 suggests that phosphorylation of this residue may underlie the PKA-induced potentiation of AMPA receptors in neurons.

Original languageEnglish (US)
Pages (from-to)1179-1188
Number of pages10
JournalNeuron
Volume16
Issue number6
DOIs
StatePublished - Jun 1996

Fingerprint

Phosphorylation
Glutamate Receptors
Neurons
AMPA Receptors
HEK293 Cells
Cyclic AMP-Dependent Protein Kinases
Protein C
Protein Kinase C
AMPA 1 glutamate receptor ionotropic

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit. / Roche, Katherine W.; O'Brien, Richard J.; Mammen, Andrew L.; Bernhardt, Jeffrey; Huganir, Richard L.

In: Neuron, Vol. 16, No. 6, 06.1996, p. 1179-1188.

Research output: Contribution to journalArticle

Roche, Katherine W. ; O'Brien, Richard J. ; Mammen, Andrew L. ; Bernhardt, Jeffrey ; Huganir, Richard L. / Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit. In: Neuron. 1996 ; Vol. 16, No. 6. pp. 1179-1188.
@article{8f07a482da1d4a8ea2024ecda4d0d5b6,
title = "Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit",
abstract = "We have characterized the phosphorylation of the glutamate receptor subunit GluR1, using biochemical and electrophysiological techniques. GluR1 is phosphorylated on multiple sites that are all located on the C-terminus of the protein. Cyclic AMP-dependent protein kinase specifically phosphorylates SER-845 of GluR1 in transfected HEK cells and in neurons in culture. Phosphorylation of this residue results in a 40{\%} potentiation of the peak current through GluR1 homomeric channels. In addition, protein kinase C specifically phosphorylates Ser-831 of GluR1 in HEK-293 cells and in cultured neurons. These results are consistent with the recently proposed transmembrane topology models of glutamate receptors, in which the C-terminus is intracellular. In addition, the modulation of GluR1 by PKA phosphorylation of Ser-845 suggests that phosphorylation of this residue may underlie the PKA-induced potentiation of AMPA receptors in neurons.",
author = "Roche, {Katherine W.} and O'Brien, {Richard J.} and Mammen, {Andrew L.} and Jeffrey Bernhardt and Huganir, {Richard L}",
year = "1996",
month = "6",
doi = "10.1016/S0896-6273(00)80144-0",
language = "English (US)",
volume = "16",
pages = "1179--1188",
journal = "Neuron",
issn = "0896-6273",
publisher = "Cell Press",
number = "6",

}

TY - JOUR

T1 - Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit

AU - Roche, Katherine W.

AU - O'Brien, Richard J.

AU - Mammen, Andrew L.

AU - Bernhardt, Jeffrey

AU - Huganir, Richard L

PY - 1996/6

Y1 - 1996/6

N2 - We have characterized the phosphorylation of the glutamate receptor subunit GluR1, using biochemical and electrophysiological techniques. GluR1 is phosphorylated on multiple sites that are all located on the C-terminus of the protein. Cyclic AMP-dependent protein kinase specifically phosphorylates SER-845 of GluR1 in transfected HEK cells and in neurons in culture. Phosphorylation of this residue results in a 40% potentiation of the peak current through GluR1 homomeric channels. In addition, protein kinase C specifically phosphorylates Ser-831 of GluR1 in HEK-293 cells and in cultured neurons. These results are consistent with the recently proposed transmembrane topology models of glutamate receptors, in which the C-terminus is intracellular. In addition, the modulation of GluR1 by PKA phosphorylation of Ser-845 suggests that phosphorylation of this residue may underlie the PKA-induced potentiation of AMPA receptors in neurons.

AB - We have characterized the phosphorylation of the glutamate receptor subunit GluR1, using biochemical and electrophysiological techniques. GluR1 is phosphorylated on multiple sites that are all located on the C-terminus of the protein. Cyclic AMP-dependent protein kinase specifically phosphorylates SER-845 of GluR1 in transfected HEK cells and in neurons in culture. Phosphorylation of this residue results in a 40% potentiation of the peak current through GluR1 homomeric channels. In addition, protein kinase C specifically phosphorylates Ser-831 of GluR1 in HEK-293 cells and in cultured neurons. These results are consistent with the recently proposed transmembrane topology models of glutamate receptors, in which the C-terminus is intracellular. In addition, the modulation of GluR1 by PKA phosphorylation of Ser-845 suggests that phosphorylation of this residue may underlie the PKA-induced potentiation of AMPA receptors in neurons.

UR - http://www.scopus.com/inward/record.url?scp=0030175899&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030175899&partnerID=8YFLogxK

U2 - 10.1016/S0896-6273(00)80144-0

DO - 10.1016/S0896-6273(00)80144-0

M3 - Article

VL - 16

SP - 1179

EP - 1188

JO - Neuron

JF - Neuron

SN - 0896-6273

IS - 6

ER -