ArticleThe Journal of biological chemistry2012
Interactions with WNK (with no lysine) family members regulate oxidative stress response 1 and ion co-transporter activity.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 25 citations in OpenAlex.
- No lysine? No problem: the surprising roles of WNK kinases in physiology and disease.The Biochemical journal · 2026Review
- Activation of WNK1 signaling through Piezo1.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The evolving concepts of KS-WNK1 effect on NCC activity.American journal of physiology. Renal physiology · 2025Review
- Unanticipated domain requirements for Drosophila Wnk kinase in vivo.PLoS genetics · 2023Article
- Hydrostatic Pressure Sensing by WNK kinases.Molecular biology of the cell · 2023Article
- Crank up the volume: Osmotic stress induces WNK1 phase separation.Cell research · 2023Article
- Looking lively: emerging principles of pseudokinase signaling.Trends in biochemical sciences · 2022Review
- UBR5 is a novel regulator of WNK1 stability.American journal of physiology. Cell physiology · 2022Article
- CCT and CCT-Like Modular Protein Interaction Domains in WNK Signaling.Molecular pharmacology · 2022Review
- Cells recognize osmotic stress through liquid-liquid phase separation lubricated with poly(ADP-ribose).Nature communications · 2021Article
- WNK1 kinase and its partners Akt, SGK1 and NBC-family NaOncotarget · 2018Article
- OSR1 regulates a subset of inward rectifier potassium channels via a binding motif variant.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Potassium-regulated distal tubule WNK bodies are kidney-specific WNK1 dependent.Molecular biology of the cell · 2018Article
- WNK1 and p38-MAPK distribution in ionocytes and accessory cells of euryhaline teleost fish implies ionoregulatory function.Biology open · 2017Article
- WNK Kinases in Development and Disease.Current topics in developmental biology · 2017Review
- Multistep regulation of autophagy by WNK1.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Hypertension: the missing WNKs.American journal of physiology. Renal physiology · 2016Review
- Inhibition of WNK3 Kinase Signaling Reduces Brain Damage and Accelerates Neurological Recovery After Stroke.Stroke · 2015Article
- Actions of the protein kinase WNK1 on endothelial cells are differentially mediated by its substrate kinases OSR1 and SPAK.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Growth attenuation under saline stress is mediated by the heterotrimeric G protein complex.BMC plant biology · 2014Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Two of the four WNK (with no lysine (K)) protein kinases are associated with a heritable form of ion imbalance culminating in hypertension. WNK1 affects ion transport in part through activation of the closely related Ste20 family protein kinases oxidative stress-responsive 1 (OSR1) and STE20/SPS1-related proline-, alanine-rich kinase (SPAK). Once activated by WNK1, OSR1 and SPAK phosphorylate and stimulate the sodium, potassium, two chloride co-transporters, NKCC1 and NKCC2, and also affect other related ion co-transporters. We find that WNK1 and OSR1 co-localize on cytoplasmic puncta in HeLa and other cell types. We show that the C-terminal region of WNK1 including a coiled coil is sufficient to localize the fragment in a manner similar to the full-length protein, but some other fragments lacking this region are mislocalized. Photobleaching experiments indicate that both hypertonic and hypotonic conditions reduce the mobility of GFP-WNK1 in cells. The four WNK family members can phosphorylate the activation loop of OSR1 to increase its activity with similar kinetic constants. C-terminal fragments of WNK1 that contain three RFXV interaction motifs can bind OSR1, block activation of OSR1 by sorbitol, and prevent the OSR1-induced enhancement of ion co-transporter activity in cells, further supporting the conclusion that association with WNK1 is required for OSR1 activation and function at least in some contexts. C-terminal WNK1 fragments can be phosphorylated by OSR1, suggesting that OSR1 catalyzes feedback phosphorylation of WNK1.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.