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dc.rights.licenseopenen_US
hal.structure.identifierNeurocentre Magendie : Physiopathologie de la Plasticité Neuronale [U1215 Inserm - UB]
dc.contributor.authorFLETCHER JONES, Alexandra
hal.structure.identifierUniversity of Bristol [Bristol]
dc.contributor.authorHILDICK, Keri L.
hal.structure.identifierUniversity of Bristol [Bristol]
dc.contributor.authorEVANS, Ashley J.
hal.structure.identifierUniversity of Bristol [Bristol]
dc.contributor.authorNAKAMURA, Yasuko
hal.structure.identifierUniversity of Bristol [Bristol]
dc.contributor.authorHENLEY, Jeremy M.
hal.structure.identifierUniversity of Bristol [Bristol]
dc.contributor.authorWILKINSON, Kevin A.
dc.date.accessioned2023-06-06T16:04:58Z
dc.date.available2023-06-06T16:04:58Z
dc.date.issued2020-06-12
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/182504
dc.description.abstractEnThe endocannabinoid system (ECS) acts as a negative feedback mechanism to suppress synaptic transmission and plays a major role in a diverse range of brain functions including, for example, the regulation of mood, energy balance, and learning and memory. The function and dysfunction of the ECS are strongly implicated in multiple psychiatric, neurological, and neurodegenerative diseases. Cannabinoid type 1 receptor (CB1R) is the most abundant G protein-coupled receptor (GPCR) expressed in the brain and, as for any synaptic receptor, CB1R needs to be in the right place at the right time to respond appropriately to changing synaptic circumstances. While CB1R is found intracellularly throughout neurons, its surface expression is highly polarized to the axonal membrane, consistent with its functional expression at presynaptic sites. Surprisingly, despite the importance of CB1R, the interacting proteins and molecular mechanisms that regulate the highly polarized distribution and function of CB1R remain relatively poorly understood. Here we set out what is currently known about the trafficking pathways and protein interactions that underpin the surface expression and axonal polarity of CB1R, and highlight key questions that still need to be addressed. In the original article, we neglected to include the funders BBSRC, (BB/R00787X/1) to JH and KWandWellcome Trust, (105384/Z/14/A) to JH and AE. The authors apologize for this error and state that this does not change the scientific conclusions of the article in any way. The original article has been updated. © 2020 Fletcher-Jones, Hildick, Evans, Nakamura, Henley and Wilkinson.
dc.language.isoENen_US
dc.rightsAttribution 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/*
dc.subject.enCannabinoid type 1 receptor
dc.subject.enEndocannabinoid system
dc.subject.enProtein-protein interactions
dc.subject.enRetrograde synaptic signaling
dc.subject.enSynaptic regulation
dc.subject.enTrafficking
dc.title.enProtein Interactors and Trafficking Pathways That Regulate the Cannabinoid Type 1 Receptor (CB1R)
dc.title.enCorrigendum: Protein Interactors and Trafficking Pathways That Regulate the Cannabinoid Type 1 Receptor (CB1R)
dc.title.alternativeFront Mol Neuroscien_US
dc.typeArticle de revueen_US
dc.identifier.doi10.3389/fnmol.2020.00142en_US
dc.subject.halSciences du Vivant [q-bio]/Neurosciences [q-bio.NC]en_US
dc.identifier.pubmed32595453en_US
bordeaux.journalFrontiers in Molecular Neuroscienceen_US
bordeaux.volume13en_US
bordeaux.hal.laboratoriesNeurocentre Magendie - U1215en_US
bordeaux.issue142en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionINSERMen_US
bordeaux.teamEndocannabinoïdes et Neuroadaptationen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-04119762
hal.version1
hal.date.transferred2023-06-06T16:05:22Z
hal.exporttrue
dc.rights.ccCC BYen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Frontiers%20in%20Molecular%20Neuroscience&rft.date=2020-06-12&rft.volume=13&rft.issue=142&rft.au=FLETCHER%20JONES,%20Alexandra&HILDICK,%20Keri%20L.&EVANS,%20Ashley%20J.&NAKAMURA,%20Yasuko&HENLEY,%20Jeremy%20M.&rft.genre=article


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