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Article

Phosphorylation by PKC and PKA regulate the kinase activity and downstream signaling of WNK4.

Proceedings of the National Academy of Sciences of the United States of America - 31 Jan 2017

Castañeda-Bueno Maria, Arroyo Juan Pablo, Zhang Junhui, Puthumana Jeremy, Yarborough Orlando, Shibata Shigeru, Rojas-Vega Lorena, Gamba Gerardo, Rinehart Jesse, Lifton Richard P

Abstract excerpt

With-no-lysine kinase 4 (WNK4) regulates electrolyte homeostasis and blood pressure. WNK4 phosphorylates the kinases SPAK (Ste20-related proline alanine-rich kinase) and OSR1 (oxidative stress responsive kinase), which then phosphorylate and activate the renal Na-Cl cotransporter (NCC). WNK4 levels are regulated by binding to Kelch-like 3, targeting WNK4 for ubiquitylation and degradation. Phosphorylation of...

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Source

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Identifiers

PMID: 28096417
DOI: 10.1073/pnas.1620315114
PMCID: PMC5293014

Genes

WNK4
OSR1

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.

Related research

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Phosphorylation by PKC and PKA regulate the kinase activity and downstream signaling of WNK4.PMID 28096417Read ↗

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SPAK deficiency corrects pseudohypoaldosteronism II caused by WNK4 mutation.Semantic proximity Read ↗

The WNK1 and WNK4 protein kinases that are mutated in Gordon's hypertension syndrome phosphorylate and activate SPAK and OSR1 protein kinases.Semantic proximity Read ↗

Serine-threonine kinase with-no-lysine 4 (WNK4) controls blood pressure via transient receptor potential canonical 3 (TRPC3) in the vasculature.Semantic proximity Read ↗

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