MAGI-1a functions as a scaffolding protein for the distal renal tubular basolateral K+ channels

Masayuki Tanemoto, Takafumi Toyohara, Takaaki Abe, Sadayoshi Ito

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)

Abstract

As the K+ recycling pathway for renal Na+ reabsorption, renal tubular K+ channels participate in the fluid and electrolyte homeostasis. Previously, we showed that the Kir5.1/Kir4.1 heteromer, which is a heteromeric assembly of two inwardly rectifying K+ channels, composes the principal basolateral K+ channels in distal renal tubules and that two motifs in the carboxyl-terminal portion of the Kir4.1 subunit regulate its functional expression. In this study, by using yeast two-hybrid screening, we identified a new isoform of membrane-associated guanylate kinase with inverted domain structure 1 (MAGI-1a-long) as a scaffolding protein for the basolateral K+ channels. MAGI-1a-long interacted with the PSD-95/Dlg/ZO-1 (PDZ)-binding motif of Kir4.1 by its fifth PDZ domain, and a high salt diet, which could suppress mineralocorticoid secretion, facilitated the interaction. The phosphorylation of serine 377 in the PDZ-binding motif disrupted the interaction, and the disruption of the interaction altered the intracellular localization of the channels from the basolateral side to perinuclear components. These results demonstrate that the phosphorylation-dependent scaffolding of the basolateral K+ channels by MAGI-1a-long participates in the renal regulation of the fluid and electrolyte homeostasis.

Original languageEnglish
Pages (from-to)12241-12247
Number of pages7
JournalJournal of Biological Chemistry
Volume283
Issue number18
DOIs
Publication statusPublished - 2008 May 2

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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