RGD Reference Report - Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains.

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Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains.
Authors:	Bouvier, Denis Spagnol, Gaelle Chenavas, Sylvie Kieken, Fabien Vitrac, Heidi Brownell, Sarah Kellezi, Admir Forge, Vincent Sorgen, Paul L
Citation:	Bouvier D, etal., J Biol Chem. 2009 Dec 4;284(49):34257-71. doi: 10.1074/jbc.M109.039594. Epub 2009 Oct 5.
RGD ID:	12793009
Pubmed:	PMID:19808665 (View Abstract at PubMed)
PMCID:	PMC2797195 (View Article at PubMed Central)
DOI:	DOI:10.1074/jbc.M109.039594 (Journal Full-text)
Gap junctions are intercellular channels that allow the passage of ions, small molecules, and second messengers that are essential for the coordination of cellular function. They are formed by two hemichannels, each constituted by the oligomerization of six connexins (Cx). Among the 21 different human Cx isoforms, studies have suggested that in the heart, Cx40 and Cx43 can oligomerize to form heteromeric hemichannels. The mechanism of heteromeric channel regulation has not been clearly defined. Tissue ischemia leads to intracellular acidification and closure of Cx43 and Cx40 homomeric channels. However, coexpression of Cx40 and Cx43 in Xenopus oocytes enhances the pH sensitivity of the channel. This phenomenon requires the carboxyl-terminal (CT) part of both connexins. In this study we used different biophysical methods to determine the structure of the Cx40CT and characterize the Cx40CT/Cx43CT interaction. Our results revealed that the Cx40CT is an intrinsically disordered protein similar to the Cx43CT and that the Cx40CT and Cx43CT can interact. Additionally, we have identified an interaction between the Cx40CT and the cytoplasmic loop of Cx40 as well as between the Cx40CT and the cytoplasmic loop of Cx43 (and vice versa). Our studies support the "particle-receptor" model for pH gating of Cx40 and Cx43 gap junction channels and suggest that interactions between cytoplasmic regulatory domains (both homo- and hetero-connexin) could be important for the regulation of heteromeric channels.

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Cellular Component

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Object Symbol	Species	Term	Qualifier	Evidence	With	Notes	Source	Original Reference(s)
Gja1	Rat	connexin complex	part_of	IMP		PMID:19808665	CAFA
Gja5	Rat	connexin complex	part_of	IMP		PMID:19808665	CAFA

Molecular Function

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Object Symbol	Species	Term	Qualifier	Evidence	With	Notes	Source	Original Reference(s)
Gja1	Rat	disordered domain specific binding	enables	IPI	UniProtKB:P28234	PMID:19808665	CAFA
Gja5	Rat	disordered domain specific binding	enables	IPI	UniProtKB:P08050	PMID:19808665	CAFA

Objects Annotated

Genes (Rattus norvegicus)

Gja1 (gap junction protein, alpha 1)

Gja5 (gap junction protein, alpha 5)

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Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains.