Gutenberg Open Science: Enhancement of phosphorylation and transport activity of the neuronal glutamate transporter excitatory amino acid transporter 3 by C3bot and a 26mer C3bot peptide

Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-8603

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DC Field	Value	Language
dc.contributor.author	Piepgras, Johannes	-
dc.contributor.author	Rohrbeck, Astrid	-
dc.contributor.author	Just, Ingo	-
dc.contributor.author	Bittner, Stefan	-
dc.contributor.author	Ahnert-Hilger, Gudrun	-
dc.contributor.author	Höltje, Markus	-
dc.date.accessioned	2023-01-20T08:57:21Z	-
dc.date.available	2023-01-20T08:57:21Z	-
dc.date.issued	2022	-
dc.identifier.uri	https://openscience.ub.uni-mainz.de/handle/20.500.12030/8619	-
dc.description.abstract	In primary murine hippocampal neurons we investigated the regulation of EAAT3-mediated glutamate transport by the Clostridium botulinum C3 transferase C3bot and a 26mer peptide derived from full length protein. Incubation with either enzyme-competent C3bot or enzyme-deficient C3bot156–181 peptide resulted in the upregulation of glutamate uptake by up to 22% compared to untreated cells. A similar enhancement of glutamate transport was also achieved by the classical phorbol-ester-mediated activation of protein kinase C subtypes. Yet comparable, effects elicited by C3 preparations seemed not to rely on PKCα, γ, ε, or ζ activation. Blocking of tyrosine phosphorylation by tyrosine kinase inhibitors prevented the observed effect mediated by C3bot and C3bot 26mer. By using biochemical and molecular biological assays we could rule out that the observed C3bot and C3bot 26mer-mediated effects solely resulted from enhanced transporter expression or translocation to the neuronal surface but was rather mediated by transporter phosphorylation at tyrosine residues that was found to be significantly enhanced following incubation with either full length protein or the 26mer C3 peptide.	en_GB
dc.description.sponsorship	Gefördert durch die Deutsche Forschungsgemeinschaft (DFG) - Projektnummer 491381577	de
dc.language.iso	eng	de
dc.rights	CC BY	*
dc.rights.uri	https://creativecommons.org/licenses/by/4.0/	*
dc.subject.ddc	610 Medizin	de_DE
dc.subject.ddc	610 Medical sciences	en_GB
dc.title	Enhancement of phosphorylation and transport activity of the neuronal glutamate transporter excitatory amino acid transporter 3 by C3bot and a 26mer C3bot peptide	en_GB
dc.type	Zeitschriftenaufsatz	de
dc.identifier.doi	http://doi.org/10.25358/openscience-8603	-
jgu.type.contenttype	Scientific article	de
jgu.type.dinitype	article	en_GB
jgu.type.version	Published version	de
jgu.type.resource	Text	de
jgu.organisation.department	FB 04 Medizin	de
jgu.organisation.number	2700	-
jgu.organisation.name	Johannes Gutenberg-Universität Mainz	-
jgu.rights.accessrights	openAccess	-
jgu.journal.title	Frontiers in cellular neuroscience	de
jgu.journal.volume	16	de
jgu.pages.alternative	860823	de
jgu.publisher.year	2022	-
jgu.publisher.name	Frontiers	de
jgu.publisher.place	Lausanne	de
jgu.publisher.issn	1662-5102	de
jgu.organisation.place	Mainz	-
jgu.subject.ddccode	610	de
jgu.publisher.doi	10.3389/fncel.2022.860823	de
jgu.organisation.ror	https://ror.org/023b0x485	-
jgu.subject.dfg	Lebenswissenschaften	de
Appears in collections:	DFG-491381577-G

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