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Article

A phosphorylation-dependent export structure in ROMK (Kir 1.1) channel overrides an endoplasmic reticulum localization signal.

The Journal of biological chemistry - 21 Oct 2005

Yoo Dana, Fang Liang, Mason Amanda, Kim Bo-Young, Welling Paul A

Abstract excerpt

The cell surface density of functional Kir1.1 (ROMK, KCNJ1) channels in the renal collecting duct is precisely regulated to maintain potassium balance. Here, we explore the mechanism by which phosphorylation of Kir1.1a serine 44 controls plasmalemma expression. Studies in Xenopus oocytes, expressing wild-type, phosphorylation mimic (S44D), or phosphorylation null (S44A) Kir1.1a, revealed that phosphorylation of...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 16118216
DOI: 10.1074/jbc.M504836200

Genes

KCNJ1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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A phosphorylation-dependent export structure in ROMK (Kir 1.1) channel overrides an endoplasmic reticulum localization signal.PMID 16118216Read ↗

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