AMPAR interacting protein CPT1C enhances surface expression of GluA1-containing receptors

AMPARs mediate the vast majority of fast excitatory synaptic transmission in the brain and their biophysical and trafficking properties depend on their subunit composition and on several posttranscriptional and posttranslational modifications. Additionally, in the brain AMPARs associate with auxilia...

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Autores: Gratacòs i Batlle, Esther, Yefimenko Nosova, Natalia, Casco García, Helena, Soto del Cerro, David
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2015
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/104026
Acceso en línea:https://hdl.handle.net/2445/104026
Access Level:acceso abierto
Palabra clave:Sinapsi
Receptors de neurotransmissors
Neurones
Electrofisiologia
Neurobiologia
Synapses
Neurotransmitter receptors
Neurons
Electrophysiology
Neurobiology
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spelling AMPAR interacting protein CPT1C enhances surface expression of GluA1-containing receptorsGratacòs i Batlle, EstherYefimenko Nosova, NataliaCasco García, HelenaSoto del Cerro, DavidSinapsiReceptors de neurotransmissorsNeuronesElectrofisiologiaNeurobiologiaSynapsesNeurotransmitter receptorsNeuronsElectrophysiologyNeurobiologyAMPARs mediate the vast majority of fast excitatory synaptic transmission in the brain and their biophysical and trafficking properties depend on their subunit composition and on several posttranscriptional and posttranslational modifications. Additionally, in the brain AMPARs associate with auxiliary subunits, which modify the properties of the receptors. Despite the abundance of AMPAR partners, recent proteomic studies have revealed even more interacting proteins that could potentially be involved in AMPAR regulation. Amongst these, carnitine palmitoyltransferase 1C (CPT1C) has been demonstrated to form an integral part of native AMPAR complexes in brain tissue extracts. Thus, we aimed to investigate whether CPT1C might be able to modulate AMPAR function. Firstly, we confirmed that CPT1C is an interacting protein of AMPARs in heterologous expression systems. Secondly, CPT1C enhanced whole-cell currents of GluA1 homomeric and GluA1/GluA2 heteromeric receptors. However, CPT1C does not alter the biophysical properties of AMPARs and co-localization experiments revealed that AMPARs and CPT1C are not associated at the plasma membrane despite a strong level of co-localization at the intracellular level. We established that increased surface GluA1 receptor number was responsible for the enhanced AMPAR mediated currents in the presence of CPT1C. Additionally, we revealed that the palmitoylable residue C585 of GluA1 is important in the enhancement of AMPAR trafficking to the cell surface by CPT1C. Nevertheless, despite its potential as a depalmitoylating enzyme, CPT1C does not affect the palmitoylation state of GluA1. To sum up, this work suggests that CPT1C plays a role as a novel regulator of AMPAR surface expression in neurons. Fine modulation of AMPAR membrane trafficking is fundamental in normal synaptic activity and in plasticity processes and CPT1C is therefore a putative candidate to regulate neuronal AMPAR physiology.Frontiers Media2016201620152016info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion17 p.application/pdfhttps://hdl.handle.net/2445/104026Articles publicats en revistes (Biomedicina)reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésReproducció del document publicat a: https://doi.org/10.3389/fncel.2014.00469Frontiers in Cellular Neuroscience, 2015, vol. 8, p. 469https://doi.org/10.3389/fncel.2014.00469info:eu-repo/grantAgreement/EC/FP7/293498cc-by (c) Gratacós i Batlle, Esther et al., 2015http://creativecommons.org/licenses/by/3.0/esinfo:eu-repo/semantics/openAccessoai:recercat.cat:2445/1040262026-05-29T05:05:01Z
dc.title.none.fl_str_mv AMPAR interacting protein CPT1C enhances surface expression of GluA1-containing receptors
title AMPAR interacting protein CPT1C enhances surface expression of GluA1-containing receptors
spellingShingle AMPAR interacting protein CPT1C enhances surface expression of GluA1-containing receptors
Gratacòs i Batlle, Esther
Sinapsi
Receptors de neurotransmissors
Neurones
Electrofisiologia
Neurobiologia
Synapses
Neurotransmitter receptors
Neurons
Electrophysiology
Neurobiology
title_short AMPAR interacting protein CPT1C enhances surface expression of GluA1-containing receptors
title_full AMPAR interacting protein CPT1C enhances surface expression of GluA1-containing receptors
title_fullStr AMPAR interacting protein CPT1C enhances surface expression of GluA1-containing receptors
title_full_unstemmed AMPAR interacting protein CPT1C enhances surface expression of GluA1-containing receptors
title_sort AMPAR interacting protein CPT1C enhances surface expression of GluA1-containing receptors
dc.creator.none.fl_str_mv Gratacòs i Batlle, Esther
Yefimenko Nosova, Natalia
Casco García, Helena
Soto del Cerro, David
author Gratacòs i Batlle, Esther
author_facet Gratacòs i Batlle, Esther
Yefimenko Nosova, Natalia
Casco García, Helena
Soto del Cerro, David
author_role author
author2 Yefimenko Nosova, Natalia
Casco García, Helena
Soto del Cerro, David
author2_role author
author
author
dc.subject.none.fl_str_mv Sinapsi
Receptors de neurotransmissors
Neurones
Electrofisiologia
Neurobiologia
Synapses
Neurotransmitter receptors
Neurons
Electrophysiology
Neurobiology
topic Sinapsi
Receptors de neurotransmissors
Neurones
Electrofisiologia
Neurobiologia
Synapses
Neurotransmitter receptors
Neurons
Electrophysiology
Neurobiology
description AMPARs mediate the vast majority of fast excitatory synaptic transmission in the brain and their biophysical and trafficking properties depend on their subunit composition and on several posttranscriptional and posttranslational modifications. Additionally, in the brain AMPARs associate with auxiliary subunits, which modify the properties of the receptors. Despite the abundance of AMPAR partners, recent proteomic studies have revealed even more interacting proteins that could potentially be involved in AMPAR regulation. Amongst these, carnitine palmitoyltransferase 1C (CPT1C) has been demonstrated to form an integral part of native AMPAR complexes in brain tissue extracts. Thus, we aimed to investigate whether CPT1C might be able to modulate AMPAR function. Firstly, we confirmed that CPT1C is an interacting protein of AMPARs in heterologous expression systems. Secondly, CPT1C enhanced whole-cell currents of GluA1 homomeric and GluA1/GluA2 heteromeric receptors. However, CPT1C does not alter the biophysical properties of AMPARs and co-localization experiments revealed that AMPARs and CPT1C are not associated at the plasma membrane despite a strong level of co-localization at the intracellular level. We established that increased surface GluA1 receptor number was responsible for the enhanced AMPAR mediated currents in the presence of CPT1C. Additionally, we revealed that the palmitoylable residue C585 of GluA1 is important in the enhancement of AMPAR trafficking to the cell surface by CPT1C. Nevertheless, despite its potential as a depalmitoylating enzyme, CPT1C does not affect the palmitoylation state of GluA1. To sum up, this work suggests that CPT1C plays a role as a novel regulator of AMPAR surface expression in neurons. Fine modulation of AMPAR membrane trafficking is fundamental in normal synaptic activity and in plasticity processes and CPT1C is therefore a putative candidate to regulate neuronal AMPAR physiology.
publishDate 2015
dc.date.none.fl_str_mv 2015
2016
2016
2016
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/104026
url https://hdl.handle.net/2445/104026
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.3389/fncel.2014.00469
Frontiers in Cellular Neuroscience, 2015, vol. 8, p. 469
https://doi.org/10.3389/fncel.2014.00469
info:eu-repo/grantAgreement/EC/FP7/293498
dc.rights.none.fl_str_mv cc-by (c) Gratacós i Batlle, Esther et al., 2015
http://creativecommons.org/licenses/by/3.0/es
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by (c) Gratacós i Batlle, Esther et al., 2015
http://creativecommons.org/licenses/by/3.0/es
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 17 p.
application/pdf
dc.publisher.none.fl_str_mv Frontiers Media
publisher.none.fl_str_mv Frontiers Media
dc.source.none.fl_str_mv Articles publicats en revistes (Biomedicina)
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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