| 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 |
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: | 17 Mar 2021 02:55 |
| URI: | https://orca.cardiff.ac.uk/id/eprint/66699 |
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