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 | |
| State | Published - Jun 1996 |
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ASJC Scopus subject areas
- Neuroscience(all)
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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 journal › Article
}
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.
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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 -