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

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

American journal of physiology. Cell physiology - 1 Sept 2010

Gagnon Kenneth B, Delpire Eric

Abstract excerpt

Threonines targeted by Ste20-related proline-alanine-rich kinase (SPAK) for phosphorylation have been identified in Na+-K+-2Cl(-) cotransporter type 1 (NKCC1), NKCC2, and Na+-Cl(-) cotransporter (NCC). However, what constitutes the substrate recognition of the kinase is still unknown. Using site-...

Read the complete abstract on PubMed

Topics

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

Share to Hydrophobic and Hydrophilic Interactions
Share to In Vitro Techniques
Share to Oocytes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Phosphorylation

Share to Protein Serine-Threonine Kinases

Share to Protein Structure, Tertiary

Share to Sodium-Potassium-Chloride Symporters

Share to Xenopus laevis

Source

Open in PubMed Open full text

Identifiers

PMID: 20463172
DOI: 10.1152/ajpcell.00074.2010
PMCID: PMC2944316

Genes

WNK4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20463172-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

On the substrate recognition and negative regulation of SPAK, a kinase modulating Na+-K+-2Cl- cotransport activity.PMID 20463172Read ↗

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

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

WNK3-SPAK interaction is required for the modulation of NCC and other members of the SLC12 family.Semantic proximity Read ↗

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.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 ↗

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 ↗

Disease-causing mutations in the acidic motif of WNK4 impair the sensitivity of WNK4 kinase to calcium ions.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 ↗

WNKs: protein kinases with a unique kinase domain.Semantic proximity Read ↗

Phosphoregulation of the intracellular termini of K+-Cl- cotransporter 2 (KCC2) enables flexible control of its activity.Semantic proximity Read ↗

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