Molecular, Structural, Functional, and Pharmacological Sites for Vesicular Glutamate Transporter Regulation.
ATPase
Glutamate (Glu)
Vesicular glutamate transporters (VGLUTs)
Journal
Molecular neurobiology
ISSN: 1559-1182
Titre abrégé: Mol Neurobiol
Pays: United States
ID NLM: 8900963
Informations de publication
Date de publication:
Jul 2020
Jul 2020
Historique:
received:
19
11
2019
accepted:
30
03
2020
pubmed:
1
6
2020
medline:
20
5
2021
entrez:
1
6
2020
Statut:
ppublish
Résumé
Vesicular glutamate transporters (VGLUTs) control quantal size of glutamatergic transmission and have been the center of numerous studies over the past two decades. VGLUTs contain two independent transport modes that facilitate glutamate packaging into synaptic vesicles and phosphate (Pi) ion transport into the synaptic terminal. While a transmembrane proton electrical gradient established by a vacuolar-type ATPase powers vesicular glutamate transport, recent studies indicate that binding sites and flux properties for chloride, potassium, and protons within VGLUTs themselves regulate VGLUT activity as well. These intrinsic ionic binding and flux properties of VGLUTs can therefore be modulated by neurophysiological conditions to affect levels of glutamate available for release from synapses. Despite their extraordinary importance, specific and high-affinity pharmacological compounds that interact with these sites and regulate VGLUT function, distinguish between the various modes of transport, and the different isoforms themselves, are lacking. In this review, we provide an overview of the physiologic sites for VGLUT regulation that could modulate glutamate release in an over-active synapse or in a disease state.
Identifiants
pubmed: 32474835
doi: 10.1007/s12035-020-01912-7
pii: 10.1007/s12035-020-01912-7
pmc: PMC7261050
doi:
Substances chimiques
Vesicular Glutamate Transport Proteins
0
Glutamic Acid
3KX376GY7L
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
3118-3142Subventions
Organisme : National Sciences and Engineering Research Council
ID : RGPIN/04682-2017
Organisme : NINDS NIH HHS
ID : R01 NS113955
Pays : United States
Organisme : Natural Sciences and Engineering Research Council
ID : RGPIN/386431-2012
Organisme : NINDS NIH HHS
ID : NS113955-01
Pays : United States
Organisme : NINDS NIH HHS
ID : R21 NS109668
Pays : United States
Organisme : Fonds de Recherche du Québec - Santé
ID : FRQS 30582
Organisme : Campus France (FR)
ID : ANR-13-SAMA-0005-01
Organisme : NINDS NIH HHS
ID : NS109668
Pays : United States
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