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PMID: 8844331 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Multiple connexin proteins in single intercellular channels: connexin compatibility and functional consequences.

Journal of bioenergetics and biomembranes ·Vol. 28 ·No. 4 ·1996-08-00 ·Pages 339-50

White TW, Bruzzone R

Abstract

In vertebrates, the protein subunits of intercellular channels found in gap junctions are encoded by a family of genes called connexins. These channels span two plasma membranes and result from the association of two half channels, or connexons, which are hexameric assemblies of connexins. Physiological analysis of channel formation and gating has revealed unique patterns of connexin-connexin interaction, and uncovered novel functional characteristics of channels containing more than one type of connexin protein. Structure-function studies have further demonstrated that unique domains within connexins participate in the regulation of different functional properties of intercellular channels. Thus, gap junctional channels can contain more than one connexin, and this structural heterogeneity has functional consequences in vitro. Moreover, emerging evidence for the existence of intercellular channels containing multiple connexins in native tissues suggests that the functional diversity generated by connexin-connexin interaction could contribute to complex communication patterns that have been observed in vivo.

MeSH Terms
Animals Connexins/physiology,ultrastructure Gap Junctions/physiology,ultrastructure Humans Ion Channel Gating Structure-Activity Relationship
Chemicals
Connexins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
White T W
Department de Morphologie, Université de Genève, Switzerland.
Bruzzone R
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Article Info
Journal
Journal of bioenergetics and biomembranes
Abbr.
J Bioenerg Biomembr
ISSN
0145-479X
DOI
10.1007/BF02110110
Published
1996-08-00
Pages
339-50
Language
English
Region
United States
NLM ID
7701859
Subset
IM
External Links
PubMed source DOI: 10.1007/BF02110110 View journal details
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