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Article: Functional analysis of selective interactions among rodent connexins

TitleFunctional analysis of selective interactions among rodent connexins
Authors
KeywordsChemicals And Cas Registry Numbers
Issue Date1995
PublisherAmerican Society for Cell Biology. The Journal's web site is located at http://www.molbiolcell.org/
Citation
Molecular Biology Of The Cell, 1995, v. 6 n. 4, p. 459-470 How to Cite?
AbstractOne consequence of the diversity in gap junction structural proteins is that cells expressing different connexins may come into contact and form intercellular channels that are mixed in connexin content. We have systematically examined the ability of adjacent cells expressing different connexins to communicate, and found that all connexins exhibit specificity in their interactions. Two extreme examples of selectivity were observed. Connexin40 (Cx40) was highly restricted in its ability to make heterotypic channels, functionally interacting with Cx37, but failing to do so when paired with Cx26, Cx32, Cx43, Cx46, and Cx50. In contrast, Cx46 interacted well with all connexins tested except Cx40. To explore the molecular basis of connexin compatibility and voltage gating, we utilized a chimera consisting of Cx32 from the N-terminus to the second transmembrane domain, fused to Cx43 from the middle cytoplasmic loop to the C-terminus. The chimeric connexin behaved like Cx43 with regard to selectivity and like Cx32 with regard to voltage dependence. Taken together, these results demonstrate that the second but not the first extracellular domain affects compatibility, whereas voltage gating is strongly influenced by sequences between the N-terminus and the second transmembrane domain.
Persistent Identifierhttp://hdl.handle.net/10722/132754
ISSN
2015 Impact Factor: 4.037
2015 SCImago Journal Rankings: 3.665
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorWhite, TWen_HK
dc.contributor.authorPaul, DLen_HK
dc.contributor.authorGoodenough, DAen_HK
dc.contributor.authorBruzzone, Ren_HK
dc.date.accessioned2011-03-28T09:28:45Z-
dc.date.available2011-03-28T09:28:45Z-
dc.date.issued1995en_HK
dc.identifier.citationMolecular Biology Of The Cell, 1995, v. 6 n. 4, p. 459-470en_HK
dc.identifier.issn1059-1524en_HK
dc.identifier.urihttp://hdl.handle.net/10722/132754-
dc.description.abstractOne consequence of the diversity in gap junction structural proteins is that cells expressing different connexins may come into contact and form intercellular channels that are mixed in connexin content. We have systematically examined the ability of adjacent cells expressing different connexins to communicate, and found that all connexins exhibit specificity in their interactions. Two extreme examples of selectivity were observed. Connexin40 (Cx40) was highly restricted in its ability to make heterotypic channels, functionally interacting with Cx37, but failing to do so when paired with Cx26, Cx32, Cx43, Cx46, and Cx50. In contrast, Cx46 interacted well with all connexins tested except Cx40. To explore the molecular basis of connexin compatibility and voltage gating, we utilized a chimera consisting of Cx32 from the N-terminus to the second transmembrane domain, fused to Cx43 from the middle cytoplasmic loop to the C-terminus. The chimeric connexin behaved like Cx43 with regard to selectivity and like Cx32 with regard to voltage dependence. Taken together, these results demonstrate that the second but not the first extracellular domain affects compatibility, whereas voltage gating is strongly influenced by sequences between the N-terminus and the second transmembrane domain.en_HK
dc.languageengen_US
dc.publisherAmerican Society for Cell Biology. The Journal's web site is located at http://www.molbiolcell.org/en_HK
dc.relation.ispartofMolecular Biology of the Cellen_HK
dc.subjectChemicals And Cas Registry Numbersen_US
dc.titleFunctional analysis of selective interactions among rodent connexinsen_HK
dc.typeArticleen_HK
dc.identifier.emailBruzzone, R: bruzzone@hkucc.hku.hken_HK
dc.identifier.authorityBruzzone, R=rp01442en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid7542941en_HK
dc.identifier.scopuseid_2-s2.0-0029020099en_HK
dc.identifier.volume6en_HK
dc.identifier.issue4en_HK
dc.identifier.spage459en_HK
dc.identifier.epage470en_HK
dc.identifier.isiWOS:A1995QW44600008-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridWhite, TW=35499703300en_HK
dc.identifier.scopusauthoridPaul, DL=7401667165en_HK
dc.identifier.scopusauthoridGoodenough, DA=7102378382en_HK
dc.identifier.scopusauthoridBruzzone, R=7006793327en_HK

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