Interactions between the Nicotinic and Endocannabinoid Receptors at the Plasma Membrane

Autores
Valles, Ana Sofia; Barrantes, Francisco Jose
Año de publicación
2022
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Compartmentalization, together with transbilayer and lateral asymmetries, provide the structural foundation for functional specializations at the cell surface, including the active role of the lipid microenvironment in the modulation of membrane-bound proteins. The chemical synapse, the site where neurotransmitter-coded signals are decoded by neurotransmitter receptors, adds another layer of complexity to the plasma membrane architectural intricacy, mainly due to the need to accommodate a sizeable number of molecules in a minute subcellular compartment with dimensions barely reaching the micrometer. In this review, we discuss how nature has developed suitable adjustments to accommodate different types of membrane-bound receptors and scaffolding proteins via membrane microdomains, and how this ?effort-sharing? mechanism has evolved to optimize crosstalk, separation, or coupling, where/when appropriate. We focus on a fast ligand-gated neurotransmitter receptor, the nicotinic acetylcholine receptor, and a second-messenger G-protein coupled receptor, the cannabinoid receptor, as a paradigmatic example.
Fil: Valles, Ana Sofia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Barrantes, Francisco Jose. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires"; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
ACETYLCHOLINE RECEPTOR
CANNABINOID RECEPTOR
CANNABINOIDS
MEMBRANE DOMAINS
NANODOMAINS
NEUROTRANSMITTER RECEPTORS
PLASMA MEMBRANE
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/203364
Acceder
id CONICETDig_fe4352f46bd61c9e552363558a08d031
oai_identifier_str oai:ri.conicet.gov.ar:11336/203364
network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling Interactions between the Nicotinic and Endocannabinoid Receptors at the Plasma MembraneValles, Ana SofiaBarrantes, Francisco JoseACETYLCHOLINE RECEPTORCANNABINOID RECEPTORCANNABINOIDSMEMBRANE DOMAINSNANODOMAINSNEUROTRANSMITTER RECEPTORSPLASMA MEMBRANEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Compartmentalization, together with transbilayer and lateral asymmetries, provide the structural foundation for functional specializations at the cell surface, including the active role of the lipid microenvironment in the modulation of membrane-bound proteins. The chemical synapse, the site where neurotransmitter-coded signals are decoded by neurotransmitter receptors, adds another layer of complexity to the plasma membrane architectural intricacy, mainly due to the need to accommodate a sizeable number of molecules in a minute subcellular compartment with dimensions barely reaching the micrometer. In this review, we discuss how nature has developed suitable adjustments to accommodate different types of membrane-bound receptors and scaffolding proteins via membrane microdomains, and how this ?effort-sharing? mechanism has evolved to optimize crosstalk, separation, or coupling, where/when appropriate. We focus on a fast ligand-gated neurotransmitter receptor, the nicotinic acetylcholine receptor, and a second-messenger G-protein coupled receptor, the cannabinoid receptor, as a paradigmatic example.Fil: Valles, Ana Sofia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaFil: Barrantes, Francisco Jose. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires"; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaMDPI2022-08-22info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/203364Valles, Ana Sofia; Barrantes, Francisco Jose; Interactions between the Nicotinic and Endocannabinoid Receptors at the Plasma Membrane; MDPI; Membranes; 12; 8; 22-8-2022; 1-192077-0375CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2077-0375/12/8/812info:eu-repo/semantics/altIdentifier/doi/10.3390/membranes12080812info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:36:09Zoai:ri.conicet.gov.ar:11336/203364instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:36:09.34CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Interactions between the Nicotinic and Endocannabinoid Receptors at the Plasma Membrane
title Interactions between the Nicotinic and Endocannabinoid Receptors at the Plasma Membrane
spellingShingle Interactions between the Nicotinic and Endocannabinoid Receptors at the Plasma Membrane
Valles, Ana Sofia
ACETYLCHOLINE RECEPTOR
CANNABINOID RECEPTOR
CANNABINOIDS
MEMBRANE DOMAINS
NANODOMAINS
NEUROTRANSMITTER RECEPTORS
PLASMA MEMBRANE
title_short Interactions between the Nicotinic and Endocannabinoid Receptors at the Plasma Membrane
title_full Interactions between the Nicotinic and Endocannabinoid Receptors at the Plasma Membrane
title_fullStr Interactions between the Nicotinic and Endocannabinoid Receptors at the Plasma Membrane
title_full_unstemmed Interactions between the Nicotinic and Endocannabinoid Receptors at the Plasma Membrane
title_sort Interactions between the Nicotinic and Endocannabinoid Receptors at the Plasma Membrane
dc.creator.none.fl_str_mv Valles, Ana Sofia
Barrantes, Francisco Jose
author Valles, Ana Sofia
author_facet Valles, Ana Sofia
Barrantes, Francisco Jose
author_role author
author2 Barrantes, Francisco Jose
author2_role author
dc.subject.none.fl_str_mv ACETYLCHOLINE RECEPTOR
CANNABINOID RECEPTOR
CANNABINOIDS
MEMBRANE DOMAINS
NANODOMAINS
NEUROTRANSMITTER RECEPTORS
PLASMA MEMBRANE
topic ACETYLCHOLINE RECEPTOR
CANNABINOID RECEPTOR
CANNABINOIDS
MEMBRANE DOMAINS
NANODOMAINS
NEUROTRANSMITTER RECEPTORS
PLASMA MEMBRANE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Compartmentalization, together with transbilayer and lateral asymmetries, provide the structural foundation for functional specializations at the cell surface, including the active role of the lipid microenvironment in the modulation of membrane-bound proteins. The chemical synapse, the site where neurotransmitter-coded signals are decoded by neurotransmitter receptors, adds another layer of complexity to the plasma membrane architectural intricacy, mainly due to the need to accommodate a sizeable number of molecules in a minute subcellular compartment with dimensions barely reaching the micrometer. In this review, we discuss how nature has developed suitable adjustments to accommodate different types of membrane-bound receptors and scaffolding proteins via membrane microdomains, and how this ?effort-sharing? mechanism has evolved to optimize crosstalk, separation, or coupling, where/when appropriate. We focus on a fast ligand-gated neurotransmitter receptor, the nicotinic acetylcholine receptor, and a second-messenger G-protein coupled receptor, the cannabinoid receptor, as a paradigmatic example.
Fil: Valles, Ana Sofia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Barrantes, Francisco Jose. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires"; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description Compartmentalization, together with transbilayer and lateral asymmetries, provide the structural foundation for functional specializations at the cell surface, including the active role of the lipid microenvironment in the modulation of membrane-bound proteins. The chemical synapse, the site where neurotransmitter-coded signals are decoded by neurotransmitter receptors, adds another layer of complexity to the plasma membrane architectural intricacy, mainly due to the need to accommodate a sizeable number of molecules in a minute subcellular compartment with dimensions barely reaching the micrometer. In this review, we discuss how nature has developed suitable adjustments to accommodate different types of membrane-bound receptors and scaffolding proteins via membrane microdomains, and how this ?effort-sharing? mechanism has evolved to optimize crosstalk, separation, or coupling, where/when appropriate. We focus on a fast ligand-gated neurotransmitter receptor, the nicotinic acetylcholine receptor, and a second-messenger G-protein coupled receptor, the cannabinoid receptor, as a paradigmatic example.
publishDate 2022
dc.date.none.fl_str_mv 2022-08-22
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/203364
Valles, Ana Sofia; Barrantes, Francisco Jose; Interactions between the Nicotinic and Endocannabinoid Receptors at the Plasma Membrane; MDPI; Membranes; 12; 8; 22-8-2022; 1-19
2077-0375
CONICET Digital
CONICET
url http://hdl.handle.net/11336/203364
identifier_str_mv Valles, Ana Sofia; Barrantes, Francisco Jose; Interactions between the Nicotinic and Endocannabinoid Receptors at the Plasma Membrane; MDPI; Membranes; 12; 8; 22-8-2022; 1-19
2077-0375
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2077-0375/12/8/812
info:eu-repo/semantics/altIdentifier/doi/10.3390/membranes12080812
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.982451

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