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dc.contributor.authorHolton, Katherine L.
dc.contributor.authorLoder, Merewyn K.
dc.contributor.authorMelikian, Haley E
dc.date2022-08-11T08:08:22.000
dc.date.accessioned2022-08-23T15:52:51Z
dc.date.available2022-08-23T15:52:51Z
dc.date.issued2005-07-01
dc.date.submitted2018-01-31
dc.identifier.citation<p>Nat Neurosci. 2005 Jul;8(7):881-8. doi: 10.1038/nn1478. <a href="https://doi.org/10.1038/nn1478">Link to article on publisher's site</a></p>
dc.identifier.issn1097-6256 (Linking)
dc.identifier.doi10.1038/nn1478
dc.identifier.pmid15924135
dc.identifier.urihttp://hdl.handle.net/20.500.14038/29231
dc.description.abstractNeurotransmitter transporters are critical for synaptic neurotransmitter inactivation. Transporter inhibitors markedly increase the duration and magnitude of synaptic transmission, underscoring the importance of transporter activity in neurotransmission. Recent studies indicate that membrane trafficking dynamically governs neuronal transporter cell-surface presentation in a protein kinase C-regulated manner, suggesting that transporter trafficking profoundly affects synaptic signaling. However, the molecular architecture coupling neurotransmitter transporters to the endocytic machinery is not defined. Here, we identify nonclassical, distinct endocytic signals in the dopamine transporter (DAT) that are necessary and sufficient to drive constitutive and protein kinase C-regulated DAT internalization. The DAT internalization signal is conserved across SLC6 neurotransmitter carriers and is functional in the homologous norepinephrine transporter, suggesting that this region is likely to be the endocytic signal for all SLC6 neurotransmitter transporters. The DAT endocytic signal does not conform to classic internalization motifs, suggesting that SLC6 neurotransmitter transporters may have evolved unique endocytic mechanisms.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=15924135&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2597780/
dc.subjectNeuroscience and Neurobiology
dc.titleNonclassical, distinct endocytic signals dictate constitutive and PKC-regulated neurotransmitter transporter internalization
dc.typeJournal Article
dc.source.journaltitleNature neuroscience
dc.source.volume8
dc.source.issue7
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/faculty_pubs/1462
dc.identifier.contextkey11452053
html.description.abstract<p>Neurotransmitter transporters are critical for synaptic neurotransmitter inactivation. Transporter inhibitors markedly increase the duration and magnitude of synaptic transmission, underscoring the importance of transporter activity in neurotransmission. Recent studies indicate that membrane trafficking dynamically governs neuronal transporter cell-surface presentation in a protein kinase C-regulated manner, suggesting that transporter trafficking profoundly affects synaptic signaling. However, the molecular architecture coupling neurotransmitter transporters to the endocytic machinery is not defined. Here, we identify nonclassical, distinct endocytic signals in the dopamine transporter (DAT) that are necessary and sufficient to drive constitutive and protein kinase C-regulated DAT internalization. The DAT internalization signal is conserved across SLC6 neurotransmitter carriers and is functional in the homologous norepinephrine transporter, suggesting that this region is likely to be the endocytic signal for all SLC6 neurotransmitter transporters. The DAT endocytic signal does not conform to classic internalization motifs, suggesting that SLC6 neurotransmitter transporters may have evolved unique endocytic mechanisms.</p>
dc.identifier.submissionpathfaculty_pubs/1462
dc.contributor.departmentMelikian Lab
dc.contributor.departmentBrudnick Neuropsychiatric Research Institute
dc.contributor.departmentDepartment of Psychiatry
dc.source.pages881-8


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