Ask about this productRelated genes to: STK39 Blocking Peptide
- Gene:
- STK39 NIH gene
- Name:
- serine/threonine kinase 39
- Previous symbol:
- -
- Synonyms:
- DCHT, SPAK
- Chromosome:
- 2q24.3
- Locus Type:
- gene with protein product
- Date approved:
- 2002-01-14
- Date modifiied:
- 2015-11-19
Related products to: STK39 Blocking Peptide
Related articles to: STK39 Blocking Peptide
- ATP2B1 and STK39 loci influence blood pressure in genome-wide association studies. We tested whether ATP2B1 rs2681472 and STK39 rs35929607 are associated with essential hypertension and blood pressure. - Source: PubMed
Akgün EgemenKaragöz AhmetMutlu İçduygu FadimeAlp Ebru - - Source: PubMed
Li ZhaoZhu WenzhuoXiong LiwenYu XiaoboChen XiLin Qiang - Lipopolysaccharide-responsive and beige-like anchor protein (LRBA) deficiency is a rare genetic disorder characterized by immune dysregulation. The immune checkpoint molecule cytotoxic T lymphocyte-associated antigen 4 (CTLA-4) fails to perform proper membrane trafficking in the absence of LRBA. In addition to immune cells, LRBA localizes to intracellular vesicles in various epithelial cells; however, its physiological roles have not been accurately deciphered. It was observed in this study that LRBA facilitates water and sodium transport by promoting vesicular trafficking of aquaporin-2 (AQP2) and AQP4 in renal collecting duct cells and that of sterile 20/SPS1-related proline/alanine-rich kinase (SPAK) in distal convoluted tubule cells. Consequently, knockout mice exhibited vasopressin-resistant polyuria and hypotension under sodium-restricted conditions. This registry study revealed a polyuric phenotype in a subset of patients with LRBA deficiency, characterized by inappropriately low urine specific gravity despite the presence of chronic diarrhea. Notably, desmopressin treatment ameliorated impaired urinary concentration in a mouse model of human LRBA deficiency. LRBA functions as a central coordinator of fluid and sodium homeostasis by organizing segment-specific vesicular trafficking systems in renal epithelial cells. - Source: PubMed
Publication date: 2026/04/28
Nagaoka KanakoAndo FumiakiFujiki TamamiAbolhassani HassanHara YuYanagawa HidekiSuzuki SoichiroSakamaki YurikoOikawa DaisukeKikuchi HiroakiMandai ShintaroMori YutaroMori TakayasuSusa KoichiroSohara EiseiHoshino AkihiroIto TsuyoshiArakawa YukiSasahara YojiYasuda ShinsukeAbe YoichiroYasui MasatoTokunaga FuminoriKanegane HirokazuUchida Shinichi - Teratozoospermia, characterized by abnormal sperm morphology, is a major contributor to male infertility. Kinases, enzymes that catalyze the transfer of phosphate groups to proteins, are crucial regulators of cellular signaling pathways and play significant roles in sperm development and maturation. The purpose of the current study was to identify differentially expressed genes (DEGs) between teratozoospermia and normozoospermia samples and to investigate the role of kinases in these expression changes. - Source: PubMed
Mousavi Seyedeh ZahraHadizadeh MortezaMohammad Soltani BahramTotonchi Mehdi - The sodium-chloride cotransporter (NCC) in the distal convoluted tubule regulates renal sodium reabsorption, potassium homeostasis, and blood pressure. NCC phosphorylation is controlled by extracellular potassium via the with-no-lysine (WNK)-STE20/SPS1-related proline-alanine-rich kinase (SPAK) kinase cascade, proposed to initiate within biomolecular condensates termed WNK bodies. Kidney-specific with-no-lysine kinase (KS-WNK1) and calcium-binding protein 39 (Cab39) play different roles in WNK body formation and dissolution. Although KS-WNK1 is required for organizing WNK bodies, previous studies suggest that Cab39 promotes SPAK translocation from the WNK bodies to the apical membrane; Cab39 deletion traps phosphorylated SPAK in intracellular puncta and suppresses NCC phosphorylation. Whether these puncta represent bona fide WNK bodies or distinct condensates is unknown. To test whether SPAK puncta require KS-WNK1, we generated mice with distal convoluted tubule-specific deletion of both Cab39 isoforms and KS-WNK1 (triple knockout). NCC, phosphorylated SPAK, and WNK4 expression and localization were assessed by immunoblotting, immunofluorescence, and quantitative (PCR) under low- and high-potassium diets that activate or inhibit the WNK-SPAK-NCC pathway. Despite elevated WNK4, triple-knockout mice exhibited marked NCC hypo-phosphorylation. Phosphorylated SPAK accumulated in cytoplasmic puncta resembling WNK bodies even without KS-WNK1, indicating they are distinct from canonical WNK bodies. Under high-potassium conditions, when WNK4 and SPAK are dephosphorylated, these puncta were absent, suggesting dependence on upstream kinase activity. Thus, SPAK puncta form independently of KS-WNK1, previously considered necessary for WNK body formation, revealing distinct signaling condensates. In this study, we identify novel biomolecular condensates (puncta) that appear in the absence of KS-WNK1, a component of WNK bodies. Mice knockout for both KS-WNK1 and Cab39 adaptor proteins exhibit large SPAK-containing puncta that also comprise WNK4 and L-WNK1. These puncta are p62-positive and ubiquitin-negative, indicating that they are sequestrating rather than degrading structures. Formation of these puncta requires active phosphorylation, as they are not observed in mice fed with a high K diet. - Source: PubMed
Publication date: 2026/03/28
Ferdaus Mohammed ZubaerulInoue Masa-KiTerker Andrew SWelling Paul ADelpire Eric