Apr 7, 2020

The dynamic Nexus: Gap junctions control protein localization and mobility in distinct and surprising ways

BioRxiv : the Preprint Server for Biology
S. McCutcheonDavid C Spray

Abstract

Gap junction (GJ) channels permit molecules, such as ions, metabolites and second messengers, to transfer between cells. Their function is critical for numerous cellular interactions. GJ channels are composed of Connexin (Cx) hexamers paired across extracellular space and typically form large rafts of clustered channels, called plaques, at cell appositions. Cxs together with molecules that interact with GJ channels make up a supramolecular structure known as the GJ Nexus. While the stability of connexin localization in GJ plaques has been studied, mobility of other Nexus components has yet to be addressed. Colocalization analysis of several nexus components and other membrane proteins reveal that certain molecules are excluded from the GJ plaque (Aquaporin 4, EAAT2b), while others are quite penetrant (lipophilic molecules, Cx30, ZO-1, Occludin). Fluorescence recovery after photobleaching (FRAP) of tagged Nexus-associated proteins showed that mobility in plaque domains is affected by mobility of the Cx proteins. These novel findings indicate that the GJ Nexus is a dynamic membrane organelle, with cytoplasmic and membrane-embedded proteins binding and diffusing according to distinct parameters.

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Mentioned in this Paper

Calcinus elegans
Cyartonema elegans
Coleonyx elegans
AN 1
Cestrum elegans
Clarkia unguiculata
Clathrulina elegans
Cardioglossa elegans
Cymbella elegans
Cyrenella elegans

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