| http://purl.uniprot.org/citations/21160027 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21160027 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21160027 | http://www.w3.org/2000/01/rdf-schema#comment | "Mammalian Ste20-like proline/alanine-rich kinase (SPAK) and oxidative stress-responsive 1 (OSR1) kinases phosphorylate and regulate cation-coupled Cl(-) cotransporter activity in response to cell volume changes. SPAK and OSR1 are activated via phosphorylation by upstream with-no-lysine (WNK) kinases. In Caenorhabditis elegans, the SPAK/OSR1 ortholog germinal center kinase (GCK)-3 binds to and regulates the activity of the cell volume- and meiotic cell cycle-dependent ClC anion channel CLH-3b. We tested the hypothesis that WNK kinases function in the GCK-3/CLH-3b signaling cascade. CLH-3b heterologously expressed in human embryonic kidney (HEK) cells was unaffected by coexpression with the single C. elegans WNK kinase, WNK-1, or kinase-dead WNK-1 dominant-negative mutants. RNA interference (RNAi) knockdown of the single Drosophila WNK kinase had no effect on the activity of CLH-3b expressed in Drosophila S2 cells. Similarly, RNAi silencing of C. elegans WNK-1 had no effect on basal or cell volume-sensitive activity of CLH-3b expressed endogenously in worm oocytes. Previous yeast 2-hybrid studies suggested that ERK kinases may function upstream of GCK-3. Pharmacological inhibition of ERK signaling disrupted CLH-3b activity in HEK cells in a GCK-3-dependent manner. RNAi silencing of the C. elegans ERK kinase MPK-1 or the ERK phosphorylating/activating kinase MEK-2 constitutively activated native CLH-3b. MEK-2 and MPK-1 play important roles in regulating the meiotic cell cycle in C. elegans oocytes. Cell cycle-dependent changes in MPK-1 correlate with the pattern of CLH-3b activation observed during oocyte meiotic maturation. We postulate that MEK-2/MPK-1 functions upstream from GCK-3 to regulate its activity during cell volume and meiotic cell cycle changes."xsd:string |
| http://purl.uniprot.org/citations/21160027 | http://purl.org/dc/terms/identifier | "doi:10.1152/ajpcell.00343.2010"xsd:string |
| http://purl.uniprot.org/citations/21160027 | http://purl.org/dc/terms/identifier | "doi:10.1152/ajpcell.00343.2010"xsd:string |
| http://purl.uniprot.org/citations/21160027 | http://purl.uniprot.org/core/author | "Miyazaki H."xsd:string |
| http://purl.uniprot.org/citations/21160027 | http://purl.uniprot.org/core/author | "Miyazaki H."xsd:string |
| http://purl.uniprot.org/citations/21160027 | http://purl.uniprot.org/core/author | "Strange K."xsd:string |
| http://purl.uniprot.org/citations/21160027 | http://purl.uniprot.org/core/author | "Strange K."xsd:string |
| http://purl.uniprot.org/citations/21160027 | http://purl.uniprot.org/core/author | "Falin R.A."xsd:string |
| http://purl.uniprot.org/citations/21160027 | http://purl.uniprot.org/core/author | "Falin R.A."xsd:string |
| http://purl.uniprot.org/citations/21160027 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21160027 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21160027 | http://purl.uniprot.org/core/name | "Am. J. Physiol."xsd:string |
| http://purl.uniprot.org/citations/21160027 | http://purl.uniprot.org/core/name | "Am. J. Physiol."xsd:string |
| http://purl.uniprot.org/citations/21160027 | http://purl.uniprot.org/core/pages | "C624-635"xsd:string |
| http://purl.uniprot.org/citations/21160027 | http://purl.uniprot.org/core/pages | "C624-635"xsd:string |
| http://purl.uniprot.org/citations/21160027 | http://purl.uniprot.org/core/title | "C. elegans STK39/SPAK ortholog-mediated inhibition of ClC anion channel activity is regulated by WNK-independent ERK kinase signaling."xsd:string |
| http://purl.uniprot.org/citations/21160027 | http://purl.uniprot.org/core/title | "C. elegans STK39/SPAK ortholog-mediated inhibition of ClC anion channel activity is regulated by WNK-independent ERK kinase signaling."xsd:string |
| http://purl.uniprot.org/citations/21160027 | http://purl.uniprot.org/core/volume | "300"xsd:string |
| http://purl.uniprot.org/citations/21160027 | http://purl.uniprot.org/core/volume | "300"xsd:string |
| http://purl.uniprot.org/citations/21160027 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21160027 |
| http://purl.uniprot.org/citations/21160027 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21160027 |
| http://purl.uniprot.org/citations/21160027 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/21160027 |
| http://purl.uniprot.org/citations/21160027 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/21160027 |