Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 103, Issue 29, Pages 10883-10888Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0604607103
Keywords
blood pressure; kinase; osmotic; stress
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Funding
- NCI NIH HHS [R33 CA107943, R21 CA107943, CA107943] Funding Source: Medline
- NIDDK NIH HHS [R01 DK034128, DK34128, R37 DK034128] Funding Source: Medline
- NIGMS NIH HHS [R01 GM053032, GM53032] Funding Source: Medline
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Oxidative stress-responsive kinase (OSR) 1 and sterile20-related, proline-, alanine-rich kinase (SPAK) are Ste20p-related protein kinases that bind to the sodium, potassium, two chloride cotransporter, NKCC. Here we present evidence that the protein kinase with no lysine [K] (WNK) 1 regulates OSR1, SPAK, and NKCC activities. OSR1 exists in a complex with WNK1 in cells, is activated by recombinant WNK1 in vitro, and is phosphorylated in a WNK1-dependent manner in cells. Depletion of WNK1 from HeLa cells by using small interfering RNA reduces OSR1 kinase activity. In addition, depletion of either WNK1 or OSR1 reduces NKCC activity, indicating that WNK1 and OSR1 are both required for NKCC function. OSR1 and SPAK are likely links between WNK1 and NKCC in a pathway that contributes to volume regulation and blood pressure homeostasis in mammals.
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