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Article: In vivo evidence for the involvement of the carboxy terminal domain in assembling connexin 36 at the electrical synapse

TitleIn vivo evidence for the involvement of the carboxy terminal domain in assembling connexin 36 at the electrical synapse
Authors
KeywordsAssembly
Connexin 36
Electrical synapse
Gap junction
Intercellular channel
Transgenic
ZO-1
Issue Date2010
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/ymcne
Citation
Molecular and Cellular Neuroscience, 2010, v. 45 n. 1, p. 47-58 How to Cite?
AbstractConnexin 36 (Cx36)-containing electrical synapses contribute to the timing and amplitude of neural responses in many brain regions. A Cx36-EGFP transgenic was previously generated to facilitate their identification and study. In this study we demonstrate that electrical coupling is normal in transgenic mice expressing Cx36 from the genomic locus and suggest that fluorescent puncta present in brain tissue represent distributed electrical synapses. These qualities emphasize the usefulness of the Cx36-EGFP reporter as a tool for the detailed anatomical characterization of electrical synapses in fixed and living tissue. However, though the fusion protein is able to form gap junctions between Xenopus laevis oocytes it is unable to restore electrical coupling to interneurons in the Cx36-deficient mouse. Further experiments in transgenic tissue and non-neural cell lines reveal impaired transport to the plasma membrane as the possible cause. By analyzing the functional deficits exhibited by the fusion protein in vivo and in vitro, we identify a motif within Cx36 that may interact with other trafficking or scaffold proteins and thereby be responsible for its incorporation into electrical synapses.
Persistent Identifierhttp://hdl.handle.net/10722/132696
ISSN
2015 Impact Factor: 3.597
2015 SCImago Journal Rankings: 2.342
PubMed Central ID
ISI Accession Number ID
Funding AgencyGrant Number
Wellcome Trust
Tenovus Scotland
Moncur Trust and Diabetes UK
Funding Information:

This study was supported by grants to SGH from The Wellcome Trust and Tenovus Scotland, and used a confocal microscope jointly funded by the Moncur Trust and Diabetes UK.

References

 

DC FieldValueLanguage
dc.contributor.authorHelbig, Ien_US
dc.contributor.authorSammler, Een_US
dc.contributor.authorEliava, Men_US
dc.contributor.authorBolshakov, APen_US
dc.contributor.authorRozov, Aen_US
dc.contributor.authorBruzzone, Ren_US
dc.contributor.authorMonyer, Hen_US
dc.contributor.authorHormuzdi, SGen_US
dc.date.accessioned2011-03-28T09:28:19Z-
dc.date.available2011-03-28T09:28:19Z-
dc.date.issued2010en_US
dc.identifier.citationMolecular and Cellular Neuroscience, 2010, v. 45 n. 1, p. 47-58en_US
dc.identifier.issn1044-7431en_US
dc.identifier.urihttp://hdl.handle.net/10722/132696-
dc.description.abstractConnexin 36 (Cx36)-containing electrical synapses contribute to the timing and amplitude of neural responses in many brain regions. A Cx36-EGFP transgenic was previously generated to facilitate their identification and study. In this study we demonstrate that electrical coupling is normal in transgenic mice expressing Cx36 from the genomic locus and suggest that fluorescent puncta present in brain tissue represent distributed electrical synapses. These qualities emphasize the usefulness of the Cx36-EGFP reporter as a tool for the detailed anatomical characterization of electrical synapses in fixed and living tissue. However, though the fusion protein is able to form gap junctions between Xenopus laevis oocytes it is unable to restore electrical coupling to interneurons in the Cx36-deficient mouse. Further experiments in transgenic tissue and non-neural cell lines reveal impaired transport to the plasma membrane as the possible cause. By analyzing the functional deficits exhibited by the fusion protein in vivo and in vitro, we identify a motif within Cx36 that may interact with other trafficking or scaffold proteins and thereby be responsible for its incorporation into electrical synapses.en_US
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/ymcneen_US
dc.relation.ispartofMolecular and Cellular Neuroscienceen_US
dc.subjectAssembly-
dc.subjectConnexin 36-
dc.subjectElectrical synapse-
dc.subjectGap junction-
dc.subjectIntercellular channel-
dc.subjectTransgenic-
dc.subjectZO-1-
dc.subject.meshAnimals-
dc.subject.meshCerebellum - metabolism - ultrastructure-
dc.subject.meshConnexins - chemistry - genetics - metabolism-
dc.subject.meshElectrical Synapses - metabolism-
dc.subject.meshHeLa Cells-
dc.titleIn vivo evidence for the involvement of the carboxy terminal domain in assembling connexin 36 at the electrical synapseen_US
dc.typeArticleen_US
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1044-7431&volume=45&issue=1&spage=47&epage=58&date=2010&atitle=In+vivo+evidence+for+the+involvement+of+the+carboxy+terminal+domain+in+assembling+connexin+36+at+the+electrical+synapse-
dc.identifier.emailBruzzone, R: bruzzone@hkucc.hku.hken_US
dc.identifier.authorityBruzzone, Roberto=rp01442en_US
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.doi10.1016/j.mcn.2010.05.008en_US
dc.identifier.pmid20510366-
dc.identifier.pmcidPMC3025355-
dc.identifier.scopuseid_2-s2.0-77955090489en_US
dc.identifier.hkuros195146-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-77955090489&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume45en_US
dc.identifier.issue1en_US
dc.identifier.spage47en_US
dc.identifier.epage58en_US
dc.identifier.isiWOS:000280698900005-
dc.identifier.citeulike7266416-

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