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PDZ binding motif-dependent localization of K⁺ channel on the basolateral side in distal tubules

¹Division of Nephrology, Hypertension and Endocrinology, Department of Medicine, and ³Division of Gastroenterological Surgery, Department of Surgery, Tohoku University Graduate School of Medicine; and ²PRESTO, Japan Science and Technology Agency

Submitted 2 June 2004 ; accepted in final form 2 August 2004

Kir5.1, a nonfunctional inwardly rectifying K⁺ channel by itself, can form functional channels by assembling with other proteins. We previously showed that Kir5.1 assembled with Kir4.1 and functioned as an acid-base regulator in the kidney. In this study, we examined the intrarenal distribution of Kir5.1 by RT-PCR analysis on dissected nephron segments and immunohistochemical analysis with the specific anti-Kir5.1 antibody. Strong expression of Kir5.1 was detected in distal convoluted tubules, and weak expression was also detected in thick ascending limb of Henle's loop. Colocalization of Kir5.1 with Kir4.1 indicated expression of Kir5.1/Kir4.1 heteromer in these nephron segments. In a renal epithelial cell line, Madin-Darby canine kidney cells, heteromer formation with Kir4.1 changed the localization of Kir5.1 from intracellular components to the cell surface. The COOH-terminal cytoplasmic portion that includes the PDZ binding motif of Kir4.1 was responsible for this intracellular localization. These data suggest the signals on the COOH terminus of Kir4.1, including PDZ binding motif, determine the intracellular localization of Kir5.1/Kir4.1 heteromer in distal tubules.

Kir5.1/Kir4.1 heteromer; renal distal tubules; intracellular localization; PDZ domain

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