Heterodimeric adenosine receptors: a device to regulate neurotransmitter release
Autor(a) principal: | |
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Data de Publicação: | 2006 |
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/10316/8506 https://doi.org/10.1007/s00018-006-6216-2 |
Resumo: | Abstract. Since 1990 it has been known that dimers are the basic functional form of nearly all G-protein-coupled receptors (GPCRs) and that homo- and heterodimerization may play a key role in correct receptor maturation and trafficking to the plasma membrane. Nevertheless, homo- and heterodimerization of GPCR has become a matter of debate especially in the search for the precise physiological meaning of this phenomenon. This article focuses on how heterodimerization of adenosine A1 and A2A receptors, which are coupled to apparently opposite signalling pathways, allows adenosine to exert a fine-tuning modulation of striatal glutamatergic neurotransmission, providing a switch mechanism by which low and high concentrations of adenosine inhibit and stimulate, respectively, glutamate release. |
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Heterodimeric adenosine receptors: a device to regulate neurotransmitter releaseAbstract. Since 1990 it has been known that dimers are the basic functional form of nearly all G-protein-coupled receptors (GPCRs) and that homo- and heterodimerization may play a key role in correct receptor maturation and trafficking to the plasma membrane. Nevertheless, homo- and heterodimerization of GPCR has become a matter of debate especially in the search for the precise physiological meaning of this phenomenon. This article focuses on how heterodimerization of adenosine A1 and A2A receptors, which are coupled to apparently opposite signalling pathways, allows adenosine to exert a fine-tuning modulation of striatal glutamatergic neurotransmission, providing a switch mechanism by which low and high concentrations of adenosine inhibit and stimulate, respectively, glutamate release.2006info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://hdl.handle.net/10316/8506http://hdl.handle.net/10316/8506https://doi.org/10.1007/s00018-006-6216-2engCellular and Molecular Life Sciences (CMLS). 63:21 (2006) 2427-2431Ciruela, F.Ferré, S.Casadó, V.Cortés, A.Cunha, R.Lluis, C.Franco, R.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:RCAAP2020-05-27T16:14:32Zoai:estudogeral.uc.pt:10316/8506Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:43:32.742292Repositório 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 |
Heterodimeric adenosine receptors: a device to regulate neurotransmitter release |
title |
Heterodimeric adenosine receptors: a device to regulate neurotransmitter release |
spellingShingle |
Heterodimeric adenosine receptors: a device to regulate neurotransmitter release Ciruela, F. |
title_short |
Heterodimeric adenosine receptors: a device to regulate neurotransmitter release |
title_full |
Heterodimeric adenosine receptors: a device to regulate neurotransmitter release |
title_fullStr |
Heterodimeric adenosine receptors: a device to regulate neurotransmitter release |
title_full_unstemmed |
Heterodimeric adenosine receptors: a device to regulate neurotransmitter release |
title_sort |
Heterodimeric adenosine receptors: a device to regulate neurotransmitter release |
author |
Ciruela, F. |
author_facet |
Ciruela, F. Ferré, S. Casadó, V. Cortés, A. Cunha, R. Lluis, C. Franco, R. |
author_role |
author |
author2 |
Ferré, S. Casadó, V. Cortés, A. Cunha, R. Lluis, C. Franco, R. |
author2_role |
author author author author author author |
dc.contributor.author.fl_str_mv |
Ciruela, F. Ferré, S. Casadó, V. Cortés, A. Cunha, R. Lluis, C. Franco, R. |
description |
Abstract. Since 1990 it has been known that dimers are the basic functional form of nearly all G-protein-coupled receptors (GPCRs) and that homo- and heterodimerization may play a key role in correct receptor maturation and trafficking to the plasma membrane. Nevertheless, homo- and heterodimerization of GPCR has become a matter of debate especially in the search for the precise physiological meaning of this phenomenon. This article focuses on how heterodimerization of adenosine A1 and A2A receptors, which are coupled to apparently opposite signalling pathways, allows adenosine to exert a fine-tuning modulation of striatal glutamatergic neurotransmission, providing a switch mechanism by which low and high concentrations of adenosine inhibit and stimulate, respectively, glutamate release. |
publishDate |
2006 |
dc.date.none.fl_str_mv |
2006 |
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/10316/8506 http://hdl.handle.net/10316/8506 https://doi.org/10.1007/s00018-006-6216-2 |
url |
http://hdl.handle.net/10316/8506 https://doi.org/10.1007/s00018-006-6216-2 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Cellular and Molecular Life Sciences (CMLS). 63:21 (2006) 2427-2431 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799133707310727168 |