ArticleAmerican journal of physiology. Cell physiology2012
Calcium-binding protein 39 facilitates molecular interaction between Ste20p proline alanine-rich kinase and oxidative stress response 1 monomers.
Article in American journal of physiology. Cell physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.
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Who cites it
24 citing papers in PubMed, 1 synthesis or guideline pooled it, 33 citations in OpenAlex.
- Common variants in UMOD associate with urinary uromodulin levels: a meta-analysis.Journal of the American Society of Nephrology : JASN · 2014Pooled it
- The kidney distal tubule potassium switch, modern diet and hypertension.Nature reviews. Nephrology · 2026Review
- Calcium-binding protein 39 in with-no-lysine kinase signaling and the modulation of renal tubular transport.Current opinion in nephrology and hypertension · 2025Review
- Navigating the multifaceted intricacies of the NaPhysiological reviews · 2024Review
- Kinase Scaffold Cab39 Is Necessary for Phospho-Activation of the Thiazide-Sensitive NCC.Hypertension (Dallas, Tex. : 1979) · 2024Article
- Intracellular CaiScience · 2024Article
- Molecular mechanisms, physiological roles, and therapeutic implications of ion fluxes in bone cells: Emphasis on the cation-ClJournal of cellular physiology · 2022Review
- CCT and CCT-Like Modular Protein Interaction Domains in WNK Signaling.Molecular pharmacology · 2022Review
- Molecular characteristics and physiological roles of NaJournal of cellular physiology · 2021Review
- WNK-SPAK/OSR1 signaling: lessons learned from an insect renal epithelium.American journal of physiology. Renal physiology · 2018Review
- WNKs on the Fly.Journal of the American Society of Nephrology : JASN · 2018Article
- Intracellular Chloride and Scaffold Protein Mo25 Cooperatively Regulate Transepithelial Ion Transport through WNK Signaling in the Malpighian Tubule.Journal of the American Society of Nephrology : JASN · 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
- Pharmacological targeting of SPAK kinase in disorders of impaired epithelial transport.Expert opinion on therapeutic targets · 2017Review
- Proteomic responses to elevated ocean temperature in ovaries of the ascidianBiology open · 2017Article
- WNK Kinases in Development and Disease.Current topics in developmental biology · 2017Review
- Hypertension: the missing WNKs.American journal of physiology. Renal physiology · 2016Review
- Osmosensation in TRPV2 dominant negative expressing skeletal muscle fibres.The Journal of physiology · 2015Article
- Structural and biochemical insights into the activation mechanisms of germinal center kinase OSR1.The Journal of biological chemistry · 2014Article
- Identification of the WNK-SPAK/OSR1 signaling pathway in rodent and human lenses.Investigative ophthalmology & visual science · 2014Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
X-ray crystallography of the catalytic domain of oxidative stress response 1 (OSR1) has provided evidence for dimerization and domain swapping. However, the functional significance of dimer formation or domain swapping has yet to be addressed. In this study, we used nine glutamine residues to link the carboxyl end of one SPAK (related Ste20 kinase) monomer to the amino end of another SPAK monomer to assess the role of kinase monomers versus dimers in Na-K-2Cl cotransporter 1 (NKCC1) activation. Transport studies in Xenopus laevis oocytes show that forcing dimerization of two wild-type SPAK molecules results in cotransporter activation when calcium-binding protein 39 (Cab39) is coexpressed, indicating that the presence of Cab39 can bypass the upstream phosphorylation requirement of SPAK normally associated with kinase activation. We determined that monomers are the functional units of the kinase as concatamers consisting of an active and various inactive monomers were still functional. Furthermore, we found that two different nonfunctional SPAK mutants could be linked together in a concatamer and activated, presumably by domain swapping, indicating that dimerization and domain swapping are both important components of kinase activation. Finally, we demonstrate rescue of a nonfunctional SPAK mutant by domain swapping with wild-type OSR1, indicating that heterodimers of the two Ste20-related kinases are possible and therefore potentially relevant to the regulation of NKCC1 activity.
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Registered trials
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.