Characterization of Phosphorylation Sites on the Glutamate Receptor 4 Subunit of the AMPA Receptors

Detalhes bibliográficos
Autor(a) principal: Carvalho, Ana Luísa
Data de Publicação: 1999
Outros Autores: Kameyama, Kimihiko, Huganir, Richard L.
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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spelling 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
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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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