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Post-translational integration and oligomerisation of connexin 26 in plasma membranes and evidence of formation of membrane pores. Implications for the assembly of gap junctions

Ahmad, Shoeb and Evans, William Howard 2002. Post-translational integration and oligomerisation of connexin 26 in plasma membranes and evidence of formation of membrane pores. Implications for the assembly of gap junctions. Biochemical Journal 365 , pp. 693-699. 10.1042/BJ20011572

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Abstract

Gap-junction channels provide a widespread intercellular signalling mechanism. They are constructed of a family of connexin membrane proteins that thread across the membrane four times and oligomerize to generate hexameric gap-junction hemichannels. Using an in vitro cell-free transcription/translation system, we demonstrate that connexin (Cx) 26, one of the smallest connexins, is integrated directly in a post-translational manner into plasma membranes. Protein-cleavage studies of Cx26 integrated into plasma membranes indicate a similar native transmembrane topography to that of Cx26 integrated co-translationally into microsomes. Cx26 integrated post-translationally into plasma membranes oligomerizes and, when incorporated into liposomes, provides permeability to ascorbic acid, suggesting that gap-junction hemichannels are generated. The results provide the basis of a novel alternative mechanism for spontaneous assembly in plasma membranes of Cx26 gap-junction hemichannels that occurs independently of the conventional biogenesis of gap junctions involving connexin trafficking and oligomerization via membrane components of the secretory pathway.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Medicine
Subjects: R Medicine > R Medicine (General)
Publisher: Biochemical Society
ISSN: 0264-6021
Last Modified: 04 Jun 2017 07:14
URI: http://orca.cf.ac.uk/id/eprint/66699

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