Characterization of Phosphorylation Sites on the Glutamate Receptor 4 Subunit of the AMPA Receptors
Autor(a) principal: | |
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Data de Publicação: | 1999 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10316/12623 https://doi.org/10.1523/jneurosci.19-12-04748.1999 |
Resumo: | Recent studies have suggested that protein phosphorylation of glutamate receptors may play an important role in synaptic transmission. Specifically, the phosphorylation of AMPA receptors has been implicated in cellular models of synaptic plasticity. The phosphorylation of the glutamate receptor 1 (GluR1) subunit of AMPA receptors by protein kinase A (PKA), protein kinase C (PKC), and Ca2+/calmodulin-dependent protein kinase II (CaMKII) has been characterized extensively. Phosphorylation of this subunit occurs exclusively on the intracellular C-terminal domain. However, the GluR1 subunit C terminus shows low homology to the other AMPA receptor subunits. In this paper we characterized the phosphorylation of AMPA receptor subunit GluR4, using site-specific mutagenesis and biochemical techniques. We found that GluR4 is phosphorylated on serine 842 within the C-terminal domain in vitro and in vivo. Serine 842 is phosphorylated by PKA, PKC, and CaMKII in vitro and is phosphorylated in transfected cells by PKA. Two-dimensional phosphopeptide analysis indicates that serine 842 is the major phosphorylation site on GluR4. In addition, we identified threonine 830 as a potential PKC phosphorylation site. These results suggest that GluR4, which is the most rapidly desensitizing AMPA receptor subunit, may be modulated by phosphorylation |
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Characterization of Phosphorylation Sites on the Glutamate Receptor 4 Subunit of the AMPA ReceptorsGlutamateAMPA receptorsGluR4PhosphorylationPKAPKCRecent studies have suggested that protein phosphorylation of glutamate receptors may play an important role in synaptic transmission. Specifically, the phosphorylation of AMPA receptors has been implicated in cellular models of synaptic plasticity. The phosphorylation of the glutamate receptor 1 (GluR1) subunit of AMPA receptors by protein kinase A (PKA), protein kinase C (PKC), and Ca2+/calmodulin-dependent protein kinase II (CaMKII) has been characterized extensively. Phosphorylation of this subunit occurs exclusively on the intracellular C-terminal domain. However, the GluR1 subunit C terminus shows low homology to the other AMPA receptor subunits. In this paper we characterized the phosphorylation of AMPA receptor subunit GluR4, using site-specific mutagenesis and biochemical techniques. We found that GluR4 is phosphorylated on serine 842 within the C-terminal domain in vitro and in vivo. Serine 842 is phosphorylated by PKA, PKC, and CaMKII in vitro and is phosphorylated in transfected cells by PKA. Two-dimensional phosphopeptide analysis indicates that serine 842 is the major phosphorylation site on GluR4. In addition, we identified threonine 830 as a potential PKC phosphorylation site. These results suggest that GluR4, which is the most rapidly desensitizing AMPA receptor subunit, may be modulated by phosphorylationSociety for Neuroscience1999-06-15info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://hdl.handle.net/10316/12623http://hdl.handle.net/10316/12623https://doi.org/10.1523/jneurosci.19-12-04748.1999engThe Journal of Neuroscience. 19:12 (1999) 4748–47541529-2401Carvalho, Ana LuísaKameyama, KimihikoHuganir, Richard L.info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2020-11-06T17:00:21Zoai:estudogeral.uc.pt:10316/12623Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:55:47.881534Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Characterization of Phosphorylation Sites on the Glutamate Receptor 4 Subunit of the AMPA Receptors |
title |
Characterization of Phosphorylation Sites on the Glutamate Receptor 4 Subunit of the AMPA Receptors |
spellingShingle |
Characterization of Phosphorylation Sites on the Glutamate Receptor 4 Subunit of the AMPA Receptors Carvalho, Ana Luísa Glutamate AMPA receptors GluR4 Phosphorylation PKA PKC |
title_short |
Characterization of Phosphorylation Sites on the Glutamate Receptor 4 Subunit of the AMPA Receptors |
title_full |
Characterization of Phosphorylation Sites on the Glutamate Receptor 4 Subunit of the AMPA Receptors |
title_fullStr |
Characterization of Phosphorylation Sites on the Glutamate Receptor 4 Subunit of the AMPA Receptors |
title_full_unstemmed |
Characterization of Phosphorylation Sites on the Glutamate Receptor 4 Subunit of the AMPA Receptors |
title_sort |
Characterization of Phosphorylation Sites on the Glutamate Receptor 4 Subunit of the AMPA Receptors |
author |
Carvalho, Ana Luísa |
author_facet |
Carvalho, Ana Luísa Kameyama, Kimihiko Huganir, Richard L. |
author_role |
author |
author2 |
Kameyama, Kimihiko Huganir, Richard L. |
author2_role |
author author |
dc.contributor.author.fl_str_mv |
Carvalho, Ana Luísa Kameyama, Kimihiko Huganir, Richard L. |
dc.subject.por.fl_str_mv |
Glutamate AMPA receptors GluR4 Phosphorylation PKA PKC |
topic |
Glutamate AMPA receptors GluR4 Phosphorylation PKA PKC |
description |
Recent studies have suggested that protein phosphorylation of glutamate receptors may play an important role in synaptic transmission. Specifically, the phosphorylation of AMPA receptors has been implicated in cellular models of synaptic plasticity. The phosphorylation of the glutamate receptor 1 (GluR1) subunit of AMPA receptors by protein kinase A (PKA), protein kinase C (PKC), and Ca2+/calmodulin-dependent protein kinase II (CaMKII) has been characterized extensively. Phosphorylation of this subunit occurs exclusively on the intracellular C-terminal domain. However, the GluR1 subunit C terminus shows low homology to the other AMPA receptor subunits. In this paper we characterized the phosphorylation of AMPA receptor subunit GluR4, using site-specific mutagenesis and biochemical techniques. We found that GluR4 is phosphorylated on serine 842 within the C-terminal domain in vitro and in vivo. Serine 842 is phosphorylated by PKA, PKC, and CaMKII in vitro and is phosphorylated in transfected cells by PKA. Two-dimensional phosphopeptide analysis indicates that serine 842 is the major phosphorylation site on GluR4. In addition, we identified threonine 830 as a potential PKC phosphorylation site. These results suggest that GluR4, which is the most rapidly desensitizing AMPA receptor subunit, may be modulated by phosphorylation |
publishDate |
1999 |
dc.date.none.fl_str_mv |
1999-06-15 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10316/12623 http://hdl.handle.net/10316/12623 https://doi.org/10.1523/jneurosci.19-12-04748.1999 |
url |
http://hdl.handle.net/10316/12623 https://doi.org/10.1523/jneurosci.19-12-04748.1999 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
The Journal of Neuroscience. 19:12 (1999) 4748–4754 1529-2401 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.publisher.none.fl_str_mv |
Society for Neuroscience |
publisher.none.fl_str_mv |
Society for Neuroscience |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
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1799133844258947072 |