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

doi:10.1016/S0896-6273(00)80144-0

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

School of Medicine

Research output: Contribution to journal › Article › peer-review

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 language	English (US)
Pages (from-to)	1179-1188
Number of pages	10
Journal	Neuron
Volume	16
Issue number	6
DOIs	https://doi.org/10.1016/S0896-6273(00)80144-0
State	Published - Jun 1996

ASJC Scopus subject areas

Neuroscience(all)

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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.}",

note = "Funding Information: We thank Drs. Lonny Levin and Randy Reed for advice on the construction of the chimeras, and Cindy Finch for help in the preparation of the manuscript. This work was supported by a training grant from the National Institutes of Health (1T32NS07368) to K. W. R., an MSTP fellowship from the National Institutes of Health to A. L. M., a CIDA grant from the National Institutes of Health to R. J. O., and a grant from the Howard Hughes Medical Institute to R. L. H. Copyright: Copyright 2017 Elsevier B.V., All rights reserved.",

year = "1996",

month = jun,

doi = "10.1016/S0896-6273(00)80144-0",

language = "English (US)",

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AU - O'Brien, Richard J.

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AU - Bernhardt, Jeffrey

AU - Huganir, Richard L.

N1 - Funding Information: We thank Drs. Lonny Levin and Randy Reed for advice on the construction of the chimeras, and Cindy Finch for help in the preparation of the manuscript. This work was supported by a training grant from the National Institutes of Health (1T32NS07368) to K. W. R., an MSTP fellowship from the National Institutes of Health to A. L. M., a CIDA grant from the National Institutes of Health to R. J. O., and a grant from the Howard Hughes Medical Institute to R. L. H. Copyright: Copyright 2017 Elsevier B.V., All rights reserved.

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.

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Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit

Abstract

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