Targeted deletion of β1-syntrophin causes a loss of K_ir 4.1 from Müller cell endfeet in mouse retina.

Proper function of the retina depends heavily on a specialized form of retinal glia called Müller cells. These cells carry out important homeostatic functions that are contingent on their polarized nature. Specifically, the Müller cell endfeet that contact retinal microvessels and the corpus vitreum show a tenfold higher concentration of the inwardly rectifying potassium channel K_ir 4.1 than other Müller cell plasma membrane domains. This highly selective enrichment of K_ir 4.1 allows K+ to be siphoned through endfoot membranes in a special form of spatial buffering. Here, we show that K_ir 4.1 is enriched in endfoot membranes through an interaction with β1-syntrophin. Targeted disruption of this syntrophin caused a loss of K_ir 4.1 from Müller cell endfeet without affecting the total level of K_ir 4.1 expression in the retina. Targeted disruption of α1-syntrophin had no effect on K_ir 4.1 localization. Our findings show that the K_ir 4.1 aggregation that forms the basis for K+ siphoning depends on a specific syntrophin isoform that colocalizes with K_ir 4.1 in Müller endfoot membranes.

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