ArticleThe Journal of biological chemistry2014
Short forms of Ste20-related proline/alanine-rich kinase (SPAK) in the kidney are created by aspartyl aminopeptidase (Dnpep)-mediated proteolytic cleavage.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- WNK4 kinase: from structure to physiology.American journal of physiology. Renal physiology · 2021Review
- Identification and characterization of alternative STK39 transcripts within human and mouse kidneys reveals species-specific regulation of blood pressure.Physiological reports · 2020Article
- C-terminally truncated, kidney-specific variants of the WNK4 kinase lack several sites that regulate its activity.The Journal of biological chemistry · 2018Article
- DNPEP is not the only peptidase that produces SPAK fragments in kidney.Physiological reports · 2017Article
- Constitutively Active SPAK Causes Hyperkalemia by Activating NCC and Remodeling Distal Tubules.Journal of the American Society of Nephrology : JASN · 2017Article
- WNK-Cab39-NKCC1 signaling increases the susceptibility to ischemic brain damage in hypertensive rats.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2017Article
- Pharmacological targeting of SPAK kinase in disorders of impaired epithelial transport.Expert opinion on therapeutic targets · 2017Review
- SPAK and OSR1 play essential roles in potassium homeostasis through actions on the distal convoluted tubule.The Journal of physiology · 2016Article
- SPAK-mediated NCC regulation in response to low-K+ diet.American journal of physiology. Renal physiology · 2015Article
- STE20/SPS1-related proline/alanine-rich kinase (SPAK) is critical for sodium reabsorption in isolated, perfused thick ascending limb.American journal of physiology. Renal physiology · 2015Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The Ste20-related kinase SPAK regulates sodium, potassium, and chloride transport in a variety of tissues. Recently, SPAK fragments, which lack the catalytic domain and are inhibitory to Na(+) transporters, have been detected in kidney. It has been hypothesized that the fragments originate from alternative translation start sites, but their precise origin is unknown. Here, we demonstrate that kidney lysate possesses proteolytic cleavage activity toward SPAK. Ion exchange and size exclusion chromatography combined with mass spectrometry identified the protease as aspartyl aminopeptidase. The presence of the protease was verified in the active fractions, and recombinant aspartyl aminopeptidase recapitulated the cleavage pattern observed with kidney lysate. Identification of the sites of cleavage by mass spectrometry allowed us to test the function of the smaller fragments and demonstrate their inhibitory action toward the Na(+)-K(+)-2Cl(-) cotransporter, NKCC2.
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