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10.1152/ajpcell.00171.2014 http://scihub22266oqcxt.onion/10.1152/ajpcell.00171.2014 C4628937!4628937 !26333598     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26333598 &cmd=llinks): Failed to open stream: HTTP request failed! 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Activation of protein kinase C? increases phosphorylation of the UT-A1 urea transporter at serine 494 in the inner medullary collecting duct |pdf=|usr=}}{{26333598 }} gab.com Text Activation of protein kinase C increases phosphorylation of the UT-A1 urea transporter at serine 494 in the inner medullary collecting duct JO: Am J Physiol Cell Physiol http://www.kidney.de/pget.php?&tw=1&pmid=26333598 #FOAvip Hypertonicity increases urea transport, as well as the phosphorylation and membrane accumulation of UT-A1, the transporter responsible for urea permeability in the inner medullary collect duct (IMCD). Hypertonicity stimulates urea transport through PKC-mediated phosphorylation. To determine whether PKC phosphorylates UT-A1, eight potential PKC phosphorylation sites were individually replaced with alanine and subsequently transfected into LLC-PK1 cells. Of the single mutants, only ablation of the S494 site dampened induction of total UT-A1 phosphorylation by the PKC activator phorbol dibutyrate (PDBu). This result was confirmed using a newly generated antibody that specifically detected phosphorylation of UT-A1 at S494. Hypertonicity increased UT-A1 phosphorylation at S494. In contrast, activators of cAMP pathways (PKA and Epac) did not increase UT-A1 phosphorylation at S494. Activation of both PKC and PKA pathways increased plasma membrane accumulation of UT-A1, although activation of PKC alone did not do so. However, ablating the PKC site S494 decreased UT-A1 abundance in the plasma membrane. This suggests that the cAMP pathway promotes UT-A1 trafficking to the apical membrane where the PKC pathway can phosphorylate the transporter, resulting in increased UT-A1 retention at the apical membrane. In summary, activation of PKC increases the phosphorylation of UT-A1 at a specific residue, S494. Although there is no cross talk with the cAMP-signaling pathway, phosphorylation of S494 through PKC may enhance vasopressin-stimulated urea permeability by retaining UT-A1 in the plasma membrane. Twit Text FOAVip Activation of protein kinase C increases phosphorylation of the UT-A1 urea transporter at serine 494 in the inner medullary collecting duct ????Am J Physiol Cell Physiol http://www.kidney.de/pget.php?&tw=1&pmid=26333598 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26333598 #FOAvip English Wikipedia <ref>{{Cite pmid|26333598 }}</ref> Activation of protein kinase C? increases phosphorylation of the UT-A1 urea transporter at serine 494 in the inner medullary collecting duct #MMPMID26333598 Blount MA ; Cipriani P ; Redd SK ; Ordas RJ ; Black LN ; Gumina DL ; Hoban CA ; Klein JD ; Sands JM Am J Physiol Cell Physiol 2015[Nov]; 309 (9 ): C608-15 PMID26333598 show ga Hypertonicity increases urea transport, as well as the phosphorylation and membrane accumulation of UT-A1, the transporter responsible for urea permeability in the inner medullary collect duct (IMCD). Hypertonicity stimulates urea transport through PKC-mediated phosphorylation. To determine whether PKC phosphorylates UT-A1, eight potential PKC phosphorylation sites were individually replaced with alanine and subsequently transfected into LLC-PK1 cells. Of the single mutants, only ablation of the S494 site dampened induction of total UT-A1 phosphorylation by the PKC activator phorbol dibutyrate (PDBu). This result was confirmed using a newly generated antibody that specifically detected phosphorylation of UT-A1 at S494. Hypertonicity increased UT-A1 phosphorylation at S494. In contrast, activators of cAMP pathways (PKA and Epac) did not increase UT-A1 phosphorylation at S494. Activation of both PKC and PKA pathways increased plasma membrane accumulation of UT-A1, although activation of PKC alone did not do so. However, ablating the PKC site S494 decreased UT-A1 abundance in the plasma membrane. This suggests that the cAMP pathway promotes UT-A1 trafficking to the apical membrane where the PKC pathway can phosphorylate the transporter, resulting in increased UT-A1 retention at the apical membrane. In summary, activation of PKC increases the phosphorylation of UT-A1 at a specific residue, S494. Although there is no cross talk with the cAMP-signaling pathway, phosphorylation of S494 through PKC may enhance vasopressin-stimulated urea permeability by retaining UT-A1 in the plasma membrane. |Animals [MESH] |Cell Membrane/drug effects/*enzymology [MESH] |Cyclic AMP-Dependent Protein Kinases/metabolism [MESH] |Cyclic AMP/metabolism [MESH] |Enzyme Activation [MESH] |Enzyme Activators/pharmacology [MESH] |Hypertonic Solutions/pharmacology [MESH] |Kidney Medulla/drug effects/*enzymology [MESH] |Kidney Tubules, Collecting/drug effects/*enzymology [MESH] |LLC-PK1 Cells [MESH] |Male [MESH] |Membrane Transport Proteins/genetics/*metabolism [MESH] |Mice [MESH] |Mutagenesis, Site-Directed [MESH] |Mutation [MESH] |Osmosis [MESH] |Phosphorylation [MESH] |Protein Kinase C-alpha/antagonists & inhibitors/*metabolism [MESH] |Protein Kinase Inhibitors/pharmacology [MESH] |Protein Transport [MESH] |Rats, Sprague-Dawley [MESH] |Serine [MESH] |Swine [MESH] |Transfection [MESH]Activation of protein kinase C? increases phosphorylation of the UT-A1(epmc).pdf DeepDyve Pubget Overpricing