Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Characterization of the interaction of the stress kinase SPAK with the Na+-K+-2Cl- cotransporter in the nervous system: evidence for a scaffolding role of the kinase.

The Journal of biological chemistry - 26 Dec 2003

Piechotta Kerstin, Garbarini Nicole, England Roger, Delpire Eric

Abstract excerpt

Activity of heterologously expressed NKCC1 was analyzed under basal and activated conditions in the presence and absence of binding of Ste20-related proline-alanine-rich kinase (SPAK). Mutant NKCC1 that lacks the ability to bind to this kinase showed K+ transport function identical to wild-type NKCC1. Thus, preventing the binding of the kinase to the cotransporter does not affect cotransporter function. In...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Biotinylation
Share to Models, Anatomic

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Nervous System

Share to p38 Mitogen-Activated Protein Kinases

Share to Sciatic Nerve

Share to Sodium-Potassium-Chloride Symporters

Share to Spinal Cord

Share to Xenopus Proteins

Source

Identifiers

PMID: 14563843
DOI: 10.1074/jbc.M309436200

Genes

OSR1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization of the interaction of the stress kinase SPAK with the Na+-K+-2Cl- cotransporter in the nervous system: evidence for a scaffolding role of the kinase.PMID 14563843Read ↗

Functional interactions of the SPAK/OSR1 kinases with their upstream activator WNK1 and downstream substrate NKCC1.Semantic proximity Read ↗

Apoptosis-associated tyrosine kinase scaffolding of protein phosphatase 1 and SPAK reveals a novel pathway for Na-K-2C1 cotransporter regulation.Semantic proximity Read ↗

SPAK/OSR1 regulate NKCC1 and WNK activity: analysis of WNK isoform interactions and activation by T-loop trans-autophosphorylation.Semantic proximity Read ↗

On the substrate recognition and negative regulation of SPAK, a kinase modulating Na+-K+-2Cl- cotransport activity.Semantic proximity Read ↗

Regulation of NKCC2 by a chloride-sensing mechanism involving the WNK3 and SPAK kinases.Semantic proximity Read ↗

SPAK and OSR1 Sensitive Kir2.1 K+ Channels.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 ↗

The regulation of salt transport and blood pressure by the WNK-SPAK/OSR1 signalling pathway.Semantic proximity Read ↗

Phosphoregulation of the Na-K-2Cl and K-Cl cotransporters by the WNK kinases.Semantic proximity Read ↗

Multiple pathways for protein phosphatase 1 (PP1) regulation of Na-K-2Cl cotransporter (NKCC1) function: the N-terminal tail of the Na-K-2Cl cotransporter serves as a regulatory scaffold for Ste20-related proline/alanine-rich kinase (SPAK) AND PP1.Semantic proximity Read ↗

With no lysine L-WNK1 isoforms are negative regulators of the K+-Cl- cotransporters.Semantic proximity Read ↗

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

⌁Select a neighboring publication to make it the new centre.